28774 |
cd01359 |
Argininosuccinate_lyase |
Argininosuccinate lyase (argininosuccinase, ASAL). This group contains proteins similar to ASAL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotleic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria. |
Argininosuccinate lyase (argininosuccinase, ASAL). This group contains proteins similar... |
true |
true |
true |
435 |
2e-160 |
560.16 |
96.78 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 22 SLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRArPQQILESDAEDIHSWVEGKLIDKVGQLGK 101
cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEA-GAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 102 KLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDES 181
cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 182 RLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNT 261
cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 262 GEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 342 AALVLDGIQVKRPRCQEAAQQGYANATELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQVIDED 420
cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420
....*....|....*....|..
1TJ7_A 421 VYPILSLQSCLDKRAAKGGVSP 442
cd01359 400 VREALDPENSVERRTSYGGTAP 421
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
0 |
28772 |
cd01334 |
Lyase_I |
Lyase class I family of the Lyase_I superfamily. This family contains proteins similar to class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), and 3-carboxy-cis,cis-muconate lactonizing (CMLE) enzyme. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. |
Lyase class I family of the Lyase_I superfamily. This family contains proteins similar... |
false |
false |
false |
330 |
1e-45 |
179.36 |
99.70 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 30 AEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESDAEDIHSWVE--GKLI-DKVGQLGKKLHTG 106
cd01334 1 IRYMVEVEVALAKALEELGLIPKSAAEEIRSAADEFSEKFKKDVKEQEGSTTHDVMAFNEvlKELIgEAGGDAARFVHYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 107 RSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA 186
cd01334 81 ATSNDVLDTAFPLAIRDALKILLPALQQLIETLAEKALKYKDVVMMGRTHLQDASPITLGQEILGWAYELKRDLDRLEEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 187 LKRLDVSPL----GCGALAGTAYEIDREQLAGWLGFASATRNSLDsVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTG 262
cd01334 161 KERVLFLGLggavGTGASTYPDPSEVRERVAKELGLAVRALNTTQ-ISERDAMVELHSALKLLAAILSKIARDIRLLSSG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 263 EAGFVELSDRVTS-GSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
cd01334 240 EIGEVKEPEAKGQgGSSAMPHKVNPIASERVTALARRVIANDESILMNLALGHLRDLVDSPVERNAIPDVVHTLTAVLET 319
|
330
....*....|
1TJ7_A 342 AALVLDGIQV 351
cd01334 320 ALGVCKGLEV 329
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
73278 |
cd01594 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
false |
false |
false |
231 |
2e-44 |
175.52 |
93.94 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 87 WVEGKLIDKVGQLGKKLH------TGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 161 QPVTFAHWCLAYVEMLARDESRLQDAlkrldvsplgcgalagtayeidreqlagwlgfasatrnsldsvsdrdHVLELLS 240
cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNK 319
cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|....
1TJ7_A 320 DMQEDKEGLFDALDTWLDCLHMAA 343
cd01594 208 DSPSMREILADSLLLLIDALRLLL 231
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28780 |
cd01597 |
pCLME |
pCLME: prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like This group contains proteins similar to pCLME, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms. |
pCLME: prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like This group... |
false |
true |
false |
437 |
4e-26 |
114.16 |
74.60 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 99 LGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLAR 178
cd01597 89 AGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 179 DESRLQDALKRLDVSPLG--CGALA--GTAYEIDREQLAGWLGFASATRNSLdsvSDRDHVLELLSAAAIGMVHLSRFAE 254
cd01597 169 HRERLDELRPRVLVVQFGgaAGTLAslGDQGLAVQEALAAELGLGVPAIPWH---TARDRIAELASFLALLTGTLGKIAR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 255 DLIFFNTGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMmtlKGLPLAYNKDM---QEDKEGLFD 330
cd01597 246 DVYLLMQTEIGEVaEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLL---DAMVQEHERDAgawHAEWIALPE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 331 ALDTWLDCLHMAALVLDGIQVKRPRCQE--AAQQGYANAtELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLS 408
cd01597 323 IFLLASGALEQAEFLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLLE 401
|
330
....*....|...
1TJ7_A 409 ELQKFSQVIDEDV 421
cd01597 402 DPEVAAYLSDEEL 414
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28773 |
cd01357 |
Aspartatase |
Aspartase_like. This group contains proteins similar to aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. |
Aspartase_like. This group contains proteins similar to aspartase (L-aspartate ammonia-.. |
false |
true |
false |
450 |
5e-24 |
107.14 |
67.78 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 186 ALKRLDVSPLGCGALaGTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAED 255
cd01357 213 ARERLREVNLGGTAI-GTGINAPPGyielvveklsEITG-LPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIAND 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 256 LIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALD 333
cd01357 290 LRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESID 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1TJ7_A 334 TWLDCLHM-AALVLDGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLPLSE 409
cd01357 370 ILTNAVRTlRERCIDGITANEERCREYVENSIGIVTALNPYI---------GYEAAAEIAKEALETGRSVRELVLEE 437
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
73279 |
cd01595 |
Adenylsuccinate_lyase_like |
Adenylsuccinate lyase_like (ASL_like): This subgroup contains proteins similar to ASL and prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE). These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting. |
Adenylsuccinate lyase_like (ASL_like): This subgroup contains proteins similar to ASL... |
false |
true |
false |
381 |
2e-21 |
99.07 |
81.36 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 88 VEGKLIDKVGQLGKK-LHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFA 166
cd01595 67 FVYALAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 167 HWCLAYVEMLARDESRLQDALKRLDVS----PLGCGALAGTAYEIDREQLAGWLGFASATRNSldSVSDRDHVLELLSAA 242
cd01595 147 KKFAVWAAELLRHLERLEEARERVLVGgisgAVGTHASLGPKGPEVEERVAEKLGLKVPPITT--QIEPRDRIAELLSAL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 243 AIGMVHLSRFAEDLIFFNTGEAGFVEL---SDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTlkgLPLAYNK 319
cd01595 225 ALIAGTLEKIATDIRLLQRTEIGEVEEpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALEN---LVQWHER 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1TJ7_A 320 DMQE---DKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQE--AAQQGYANATELADYLVAKGVPFREAHHIVGEA 391
cd01595 300 DLSDssvERNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRnlDLTWGLILSEAVMMALAKKGLGRQEAYELVKEE 376
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28779 |
cd01596 |
Aspartatase_like |
Aspartase_like. This group contains proteins similar to aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle. |
Aspartase_like. This group contains proteins similar to aspartase (L-aspartate ammonia-.. |
false |
true |
false |
450 |
2e-21 |
98.99 |
66.44 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 108 SRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDAL 187
cd01596 135 SNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 188 KRLDVSPLGcGALAGTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLI 257
cd01596 215 ERLRELNLG-GTAVGTGLNAPPGyaekvaaelaELTG-LPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 258 FFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKG--------LPL-AYNkdmqedke 326
cd01596 292 LLSSGpRAGLGEINlPANQPGSSIMPGKVNPVIPEAVNMVAAQVIGNDTAITMAGSAgqlelnvfKPViAYN-------- 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1TJ7_A 327 gLFDALDTWLD-CLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGVPFREA 384
cd01596 364 -LLQSIRLLANaCRSFRDKCVEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
73260 |
cd01360 |
Adenylsuccinate_lyase_1 |
Adenylsuccinate lyase_1: Adenylsuccinate lyase (ASL)_subgroup 1. This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). |
Adenylsuccinate lyase_1: Adenylsuccinate lyase (ASL)_subgroup 1. This subgroup... |
false |
true |
false |
387 |
2e-18 |
89.05 |
83.72 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 69 VRARPQQILESDAE---DIHSWVEGkLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQN 145
cd01360 49 AKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 146 NQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGcGALaGTAYEID---REQLAGWLGFASAT 222
cd01360 128 HKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKIS-GAV-GTYANLGpevEERVAEKLGLKPEP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 223 RNSldSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCgRVQG 301
cd01360 206 IST--QVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVLEVeEPFSKGQKGSSAMPHKRNPILSENICGLA-RVIR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 302 ALTGMMMtlKGLPLAYNKDMQE---DKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQE--AAQQGYANATELADYLVA 376
cd01360 283 SNVIPAL--ENVALWHERDISHssvERVILPDATILLDYILRRMTRVLENLVVYPENMRRnlNLTKGLIFSQRVLLALVE 360
|
330
....*....|..
1TJ7_A 377 KGVPFREAHHIV 388
cd01360 361 KGMSREEAYEIV 372
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28776 |
cd01362 |
Fumarase_classII |
Class II fumarases. This group contains proteins similar to Escherichia coli fumarase C and the human mitochondrial fumarase. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle. |
Class II fumarases. This group contains proteins similar to Escherichia coli fumarase... |
false |
true |
false |
455 |
1e-16 |
83.25 |
66.37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRNDQVATDLKLWCKDTVSE-LLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
cd01362 133 SQSSNDTFPTAMHIAAALALQErLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 185 DALKRLDVSPLGcGALAGTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAE 254
cd01362 213 AALPRLYELALG-GTAVGTGLNAHPGfaekvaaelaELTG-LPFVTAP-NKFEALAAHDALVEASGALKTLAVSLMKIAN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 255 DLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQG--------ALTGMMMTLKGLPL-AYNkdMQE 323
cd01362 290 DIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNPTQCEALTMVAAQVMGndaaitiaGSSGNFELNVFKPViIYN--LLQ 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1TJ7_A 324 DKEGLFDAldtwldCLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGVPFREA 384
cd01362 368 SIRLLADA------CRSFADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 434
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
109271 |
pfam00206 |
Lyase_1 |
Lyase |
Lyase |
false |
false |
false |
311 |
1e-92 |
335.47 |
100.00 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 6 GRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESDAEDIH 85
pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLSEEDIKGLAALKKAAAKANVLLKEEAAAIIKALDEVAEEGKADDAFVLDVIQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 86 SWVEGKLIDKVGQL------GKKLHTGRSRNDQVATDLKLWCKDTVSE-LLTANRQLQSALVETAQNNQDAVMPGYTHLQ 158
pfam00206 81 TAVNMNLNEVIGELlgqvhpNDKVHTGQSSNDQVPTALRLALKLALSEvLLPALGQLIDALKEKAKEFADVVKPGRTHLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 159 RAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDRE---QLAGWLGFASA----TRNSLDSVSD 231
pfam00206 161 DATPVTLGQELSGYAVALTRDLERLKQLLPRILVEPLGGGTAVGTGLNADPEfaeLLAKELGFFTGlpvpAPNSFEATSD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1TJ7_A 232 RDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQG 301
pfam00206 241 RDAVVEFSGALALLATHLSKFANDLRLLSSGPFGFVELSLPEgEPGSSIMPGKVNPDQLELLRGKAGRVFG 311
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
102095 |
PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
false |
false |
false |
352 |
6e-07 |
50.47 |
53.98 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 100 GKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
PRK05975 99 AAHVHFGATSQDVIDTSLMLRLKAASEILAARLGQLIEALDALEATFGGNALTGHTRMQAAIPITVADRLESWRAPLARH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 180 ESRLQDAlkRLDVSPLGCGALAGTAYEID------REQLAGWLGFASATR--NSLDSVSDRDHVLELLSAAaigmvhLSR 251
PRK05975 179 RDRLEAL--RPDVFPLQFGGAAGTLEKLGgkaaavRAELAKRLGLEDAPQwhSQRDFIADFGHLLSLVTGS------LGK 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
1TJ7_A 252 FAEDLiffntgeAGFVELSDRVT----SGSSLMPQKKNPDALELI 292
PRK05975 251 FGQDI-------ALMAQLGDEISlsggGGSSAMPHKQNPVAAEIL 288
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28782 |
cd03302 |
Adenylsuccinate_lyase_2 |
Adenylsuccinate lyase_2: Adenylsuccinate lyase (ASL)_subgroup 2. This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting. |
Adenylsuccinate lyase_2: Adenylsuccinate lyase (ASL)_subgroup 2. This subgroup... |
false |
true |
false |
436 |
2e-04 |
42.56 |
41.28 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 115 TDLkLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDV-- 192
cd03302 103 TDL-IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFrg 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 193 --SPLGCGALAGTAYEIDREQ-------LAGWLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFntge 263
cd03302 182 vkGTTGTQASFLDLFEGDHDKvealdelVTKKAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL---- 256
|
170 180
....*....|....*....|....*.
1TJ7_A 264 AGFVELSDRVTS---GSSLMPQKKNP 286
cd03302 257 ANLKEVEEPFEKgqiGSSAMPYKRNP 282
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
28781 |
cd01598 |
PurB |
PurB: PurB_like adenylosuccinases (adenylsuccinate lyase, ASL). This group contains proteins similar to EcASL, the product of the gene purB in Escherichia coli. ASL is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). |
PurB: PurB_like adenylosuccinases (adenylsuccinate lyase, ASL). This group contains... |
false |
true |
false |
425 |
6e-04 |
40.59 |
47.29 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 93 IDKVGQLGKKL---HTGRSRNDQVATDLKLWCKDTVSELLTAN-RQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHW 168
cd01598 82 FETLGLLKKIKefiHFACTSEDINNLAYALMIKEARNEVILPLlKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 169 CLAYVEmlardesRLQDALKRLDVSPLgCGALAGT---------AY-EIDreqlagWLGFASATRNSLD--------SVS 230
cd01598 162 LAVFVY-------RLERQYKQLKQIEI-LGKFNGAvgnfnahlvAYpDVD------WRKFSEFFVTSLGltwnpyttQIE 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1TJ7_A 231 DRDHVLELLSAaaigmvhLSRFAEDLIFFNTGEAGFVEL--------SDRVtsGSSLMPQKKNP 286
cd01598 228 PHDYIAELFDA-------LARINTILIDLCRDIWGYISLgyfkqkvkKGEV--GSSTMPHKVNP 282
|
|
cl00013 |
119453 |
Lyase_I_like |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively. |
Lyase class I_like. Lyase class I_like superfamily of enzymes that catalyze beta-... |
-1 |
101572 |
PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
argininosuccinate lyase; Provisional |
true |
true |
false |
457 |
< 1.0e-180 |
916.36 |
96.72 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSIAWSKALVTVGVLTAEEQQQLEQALNELLEEVRANPQAILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
PRK04833 81 AEDIHSWVESKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVTELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
PRK04833 161 QPVTFAHWCLAYVEMLERDESRLQDALKRLDVSPLGSGALAGTAYAIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVNRPRCLEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1TJ7_A 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSP 442
PRK04833 401 PLEDLPLAELQKFSAVIGDDVYPILSLQSCLDKRAAKGGVSP 442
|
|
|
|
|
|
|
-1 |
105529 |
PRK12308 |
PRK12308 |
bifunctional argininosuccinate lyase/N-acetylglutamate synthase; Provisional |
bifunctional argininosuccinate lyase/N-acetylglutamate synthase; Provisional |
false |
true |
false |
616 |
< 1.0e-180 |
779.35 |
71.75 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSAEEQQKLEAALNELKLEVMEDPEQILRSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
PRK12308 81 AEDIHSWVEQQLIEKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNLAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHSLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1TJ7_A 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSP 442
PRK12308 401 ALEDLSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSP 442
|
|
|
|
|
|
|
-1 |
100696 |
PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
argininosuccinate lyase; Provisional |
false |
true |
false |
459 |
< 1.0e-180 |
642.23 |
96.08 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
PRK00855 4 NKLWGGRFSGGPDALVERFTASIEFDKRLAEEDIAGSIAHATMLAKQGILSEEEAEKILAGLDEILEEIEAGEFEFSVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
PRK00855 84 -EDIHMAIEARLIERIGDAGGKLHTGRSRNDQVATDLRLYLRDKIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
PRK00855 163 QPVTFGHHLLAYAEMLERDLERLRDARKRVNRSPLGAAALAGTSFPIDRERTAELLGFDGVYENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
PRK00855 243 AASLLMVHLSRLAEELILWSSPEFGFVTLPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGHLTGLLTVMKGLPLAYNKD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
PRK00855 323 LQEDKEPLFDAVDTLKDSLEAMAGMLETLTVNKERMREAAEKGFSTATDLADYLVRKGVPFRDAHEIVGKAVKEAEEKGV 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1TJ7_A 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSP 442
PRK00855 403 DLADLSLEELQAISPLITEDVYEVLTPEGSVAARNSYGGTAP 444
|
|
|
|
|
|
|
-1 |
30514 |
COG0165 |
ArgH |
Argininosuccinate lyase [Amino acid transport and metabolism] |
Argininosuccinate lyase [Amino acid transport and metabolism] |
false |
true |
false |
459 |
1e-178 |
621.49 |
96.08 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARpQQILESD 80
COG0165 3 NKLWGGRFSGGPDPLVKEFNASISFDKRLAEYDIAGSIAHAKMLAKQGIITEEEAAKILEGLEELLEEIRAG-KFELDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
COG0165 82 DEDVHTAIEARLIERIGDVGGKLHTGRSRNDQVATDLRLWLRDKLLELLELIRILQKALLDLAEEHAETVMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
COG0165 162 QPVTFAHHLLAYAEMLARDIERLRDALKRVNVSPLGAGALAGTPFPIDRERTAELLGFDAVTRNSLDAVSDRDFILEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
COG0165 242 AAALIMVHLSRLAEDLILWSSPEFGFIELPDEFSTGSSIMPQKKNPDVLELIRGKAGRVIGALTGLLTIMKGLPLAYNRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
COG0165 322 LQEDKEPLFDSVDTLEDSLRVLAGMVSGLTVNKERMREAAEAGFSTATDLADYLVRKGVPFREAHEIVGEAVRRAEERGK 401
|
410 420 430 440
....*....|....*....|....*....|....*....|..
1TJ7_A 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSP 442
COG0165 402 DLADLSLEELQSISPLIDEDVYEVLTPEESVAKRNSEGGTAP 443
|
|
|
|
|
|
|
-1 |
100996 |
PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
argininosuccinate lyase; Provisional |
false |
true |
false |
892 |
4e-55 |
210.88 |
38.57 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 70 RARPQQILESDA-EDIHSWVEGKLIDKVGQ-LGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQ 147
PRK02186 480 DAGFAPLLARPApRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANV 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 148 DAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLD 227
PRK02186 560 DCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLD 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 228 SVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMM 307
PRK02186 640 AVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASAS 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 308 MTLKGLPlaYNKDMQEDKEG---LFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVA-KGVPFRE 383
PRK02186 720 AALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDGGVSATAVAESLVVrRSISFRS 797
|
330 340
....*....|....*....|....*..
1TJ7_A 384 AHHIVGEAVVEAIRQGKPLEDlPLSEL 410
PRK02186 798 AHTQVGQAIRQSLDQGRSSAD-ALAAL 823
|
|
|
|
|
|
|
-1 |
102508 |
PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
argininosuccinate lyase; Provisional |
false |
true |
false |
502 |
1e-43 |
172.89 |
69.12 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 103 LHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESR 182
PRK06705 110 MHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLER 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 183 LQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTG 262
PRK06705 190 MKKTYKLLNQSPMGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 263 EAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEG-LFDALDTWLDCLHM 341
PRK06705 270 EYDGITVARPYVQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 342 AALVLDGIQVKRPRCQEAAQQGYANATELADYLVAK-GVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQ----- 415
PRK06705 350 LNAVIRTMKVEEDTLKRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQekfki 429
|
330 340
....*....|....*....|....*..
1TJ7_A 416 -VIDEDVYPILSLQSCLDKRAAKGGVS 441
PRK06705 430 qLLEKEWEEIISPEAFIQKRNVYGGPS 456
|
|
|
|
|
|
|
-1 |
102352 |
PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
argininosuccinate lyase; Provisional |
false |
true |
false |
434 |
3e-32 |
134.64 |
80.65 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 77 LESDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELltaNRQLQSALVETAQNNQDAVMPGYTH 156
PRK06389 74 IDLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEI---EKILYEIIKVIPGFNLKGRLPGYTH 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 157 LQRAQPVTFAHWcLAYVE-MLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHV 235
PRK06389 151 FRQAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 236 LELLSAAAIG-MVHLSRFAEDLIffNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLP 314
PRK06389 230 IENISYLISSlAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 315 LAYNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPrcQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAV-- 392
PRK06389 308 TGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEIT--NEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIre 385
|
330 340 350
....*....|....*....|....*....|....*...
1TJ7_A 393 ---VEAIRQGKPLEDLPLSELQKFSQVIDEDVYPILSL 427
PRK06389 386 gevLDEYQPEDLTDYIDVNELKRINHNIKIIIEPREKL 423
|
|
|
|
|
|
|
-1 |
31230 |
COG1027 |
AspA |
Aspartate ammonia-lyase [Amino acid transport and metabolism] |
Aspartate ammonia-lyase [Amino acid transport and metabolism] |
false |
true |
false |
471 |
8e-23 |
103.40 |
64.76 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
COG1027 139 SQSTNDAYPTAFRIAVYKSLRKLIDALEDLIEAFERKAKEFADILKMGRTQLQDAVPMTLGQEFGAFAVALKEDIKRIYR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 186 ALKRLDVSPLGcGALAGTAYEIDR-------EQLAGWLGFA-SATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLI 257
COG1027 219 AAELLLEVNLG-GTAIGTGINAPKgyielvvKKLAEVTGLPlVPAENLIEATQDTGAFVMVSGALKRLAVKLSKICNDLR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 258 FFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTW 335
COG1027 298 LLSSGpRAGLNEINlPAVQAGSSIMPGKVNPVIPEVVNQVCFKVIGNDTTITMAAEAGQLQLNVMEPVIAYALFESISIL 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1TJ7_A 336 LD-CLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLPLSE 409
COG1027 378 TNaCRNLREKCIDGITANEERCEEYVENSIGIVTALNPYI---------GYENAAIIAKEALETGKSVREVVLER 443
|
|
|
|
|
|
|
-1 |
106311 |
PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
aspartate ammonia-lyase; Provisional |
false |
true |
false |
473 |
1e-21 |
99.31 |
65.75 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
PRK13353 138 AQSTNDVFPTAIRIATLNLLEGLLQAMGALHDVFEEKAEEFDHVIKMGRTHLQDAVPIRLGQEFSAYARVLERDMKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 186 ALKRLDVSPLGCGALaGTAYEIDRE-------QLAGWLGFA-SATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLI 257
PRK13353 218 SREHLYEVNLGATAV-GTGLNADPEyieavvkHLAAISGLPlVGAEDLVDATQNTDAYVEVSAALKVCAMNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 258 FFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYN-------KDMQEDKEGL 328
PRK13353 297 LLASGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVINQIAFQVIGNDHTICLAAEAGQLELNvmepviaFNLLQSIEIL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 329 FDALDTWLD-ClhmaalvLDGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLPL 407
PRK13353 377 TNGFRAFTDnC-------VKGIEANEERCKEYVEKSVGIITALNPHI---------GYEAAARIAKEAIATGRSVRELCL 440
|
330
....*....|...
1TJ7_A 408 SElqkfsQVIDED 420
PRK13353 441 EN-----GVLTEE 448
|
|
|
|
|
|
|
-1 |
30365 |
COG0015 |
PurB |
Adenylosuccinate lyase [Nucleotide transport and metabolism] |
Adenylosuccinate lyase [Nucleotide transport and metabolism] |
false |
true |
false |
438 |
3e-21 |
98.39 |
74.66 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 100 GKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
COG0015 89 SEYVHFGATSQDIIDTALALQLKEALDLILPDLKRLIEALAELALEHKDTPMLGRTHGQPAEPTTFGKKFANWLAELLRH 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 180 ESRLQDALKRLDVSPLG--CGALA--GTAYEIDREQLAGWLGFASATRNSldSVSDRDHVLELLSAAAIGMVHLSRFAED 255
COG0015 169 LERLEEAEERIIVGKIGgaVGTLAalGDLGAEVEERVAEKLGLKPAPIST--QVSPRDRIAEFFSALALLAGSLEKFARD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 256 L-IFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLkglPLAYNKDMQE---DKEGLFDA 331
COG0015 247 IrLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENVTGLARVARALVSTLLENL---VLWHERDLTDssvERVILPDA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 332 LDTWLDCLHMAALVLDGIQVKRPRCQE--AAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLSE 409
COG0015 324 FIAADGALNRLLNVLEGLEVNPERMRRnlDLTLGLIASERVMLALRKKGMGREEAHELVREKAMKAWEQGKEFLELLLAD 403
|
330
....*....|..
1TJ7_A 410 LQKFSQVIDEDV 421
COG0015 404 ERVTKYLSEEEL 415
|
|
|
|
|
|
|
-1 |
103615 |
PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
adenylosuccinate lyase; Provisional |
false |
true |
false |
438 |
5e-18 |
87.47 |
80.82 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 73 PQQILESDAEDIHSWV--EGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAV 150
PRK08937 56 IERIAEIEKETRHDVVafLEALNEQLGEAGKWVHLGMTSTDVVDTALSLQIKEALDLIRKKLENVIGRLAKLALEYKETV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 151 MPGYTHLQRAQPVTFAH-WCLAYVEMLaRDESRLQDALKRLDV----SPLGCGALAGTAYEIDREQLAGWLGFASAtrNS 225
PRK08937 136 MMGRTHGLHAEPTTFGKkFALWYDELL-RHLERLKEAFKRVEVgkisGAVGTYANLLPLLAELEKYVAEKLGLESD--DV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 226 LDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTS-GSSLMPQKKNPDALELIRGkCGRVQGALT 304
PRK08937 213 STQVYPRDLHAEYISTLALIATSAERFAVEIRLLQRSEIREVEEGFAKGQkGSSAMPHKRNPISSENITG-LARVLRGYV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 305 GMMMTLKGLPLAY-NKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQ-EAAQQGYANATE-LADYLVAKGVPF 381
PRK08937 292 VTAYENVPLWHERdISHSSAERIALPDAFLALDYMLNRFLNLLDNLVVFPENIErNLDRTLGFIATErVLLALVNKGMGR 371
|
330 340 350
....*....|....*....|....*....|....*....
1TJ7_A 382 REAHHIVGEAVVEAIRQGKPLEDLpLSELQKFSQVIDED 420
PRK08937 372 EDAYELVQEKAMALAKTYVDLRER-LEADERFEKQLAYE 409
|
|
|
|
|
|
|
-1 |
30463 |
COG0114 |
FumC |
Fumarase [Energy production and conversion] |
Fumarase [Energy production and conversion] |
false |
true |
false |
462 |
6e-17 |
84.11 |
65.37 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRNDQVATDLKLWC-KDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
COG0114 136 SQSSNDTFPTAMHIAAvLAVVNRLIPALKHLIKTLAAKAEEFADVVKIGRTHLQDATPLTLGQEFSGYAAQLEHALERIE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 185 DALKRLDVSPLGcGALAGTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAE 254
COG0114 216 ASLPHLYELAIG-GTAVGTGLNAHPEfgekvaeelaELTG-LPFVTAP-NKFEALAAHDALVEASGALRTLAVSLMKIAN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 255 DLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQG--------ALTGMMMTLKGLPL-AYNkdMQE 323
COG0114 293 DIRWLGSGpRCGLGEIElPENEPGSSIMPGKVNPTQCEALTMVAAQVIGndaaiafaGSQGNFELNVFKPViAYN--FLQ 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1TJ7_A 324 DKEGLFDAldtwldCLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGVPFREA 384
COG0114 371 SVRLLADA------MRSFADHCIVGIEPNEERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGTTLREA 437
|
|
|
|
|
|
|
-1 |
105494 |
PRK12273 |
aspA |
aspartate ammonia-lyase; Provisional |
aspartate ammonia-lyase; Provisional |
false |
true |
false |
470 |
8e-14 |
73.66 |
64.47 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 108 SRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVT----FAhwclAYVEMLARDESRL 183
PRK12273 141 STNDAYPTAIRIALLLSLRKLLDALEELQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqeFG----AFAVALAEDIKRL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 184 QDALKRLDVSPLGcgalaGTA----------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHL 249
PRK12273 217 EEAAELLREVNLG-----ATAigtginappgYiELVVKKLAeitG-LPLVPAE-DLIEATQDCGAFVEVSGALKRLAVKL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 250 SRFAEDLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGA-LTGMMMTLKG-------LPL-AYN 318
PRK12273 290 SKICNDLRLLSSGpRAGLNEINlPAVQPGSSIMPGKVNPVIPEVVNQVCFQVIGNdTTVTMAAEAGqlqlnvmEPViAYA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 319 kdmqedkegLFDALDtWLD--CLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAI 396
PRK12273 370 ---------LFESIS-ILTnaCRTLREKCIDGITANEERCREYVENSIGIVTALNPYI---------GYENAAEIAKEAL 430
|
330
....*....|...
1TJ7_A 397 RQGKPLEDLPLSE 409
PRK12273 431 ETGKSVRELVLER 443
|
|
|
|
|
|
|
-1 |
103664 |
PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
false |
true |
false |
439 |
3e-12 |
68.56 |
69.25 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 104 HTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRL 183
PRK09053 93 HWGATSQDIIDTGLVLQLRDALDLLEPDLRRLCAALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALTRHRQRL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 184 QDALKRLDVspLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSV---SDRDHVLELlsAAAIGMV--HLSRFAEDLIF 258
PRK09053 173 AALRPRALV--LQFGGAAGTLASLGEQALAVAQALAEELQLALPAQpwhTQRDRIVEF--ASALGLLagTLGKIARDVSL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 259 FNTGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMmmtLKGLPlaynkdmQEDKEGL------FDA 331
PRK09053 249 LMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATL---FAAMV-------QEHERALggwhaeWDT 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 332 LDTwLDCLHMAAL-----VLDGIQVKRPRCQE--AAQQG--YANATELAdylVAKGVPFREAHHIVGEAVVEAIRQGKPL 402
PRK09053 319 LPE-LACLASGALaqmaqIVEGLEVDAARMRAnlDLTHGlvLAEAVMLA---LADRIGRLDAHHLVEQASKRAVAQGRHL 394
|
..
1TJ7_A 403 ED 404
PRK09053 395 RD 396
|
|
|
|
|
|
|
-1 |
100575 |
PRK00485 |
fumC |
fumarate hydratase; Reviewed |
fumarate hydratase; Reviewed |
false |
true |
false |
464 |
2e-11 |
65.90 |
65.09 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 106 GRSRND------QVATDLKLwckdtVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
PRK00485 137 SQSSNDtfptamHIAAALAI-----EERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 180 ESRLQDALKRLDVSPLGcGALAGT------------AYEIdrEQLAGwLGFASAtRNSLDSVSDRDHVLEL---LSAAAi 244
PRK00485 212 IERIEAALPHLYELALG-GTAVGTglnahpgfaekvAAEL--AELTG-LPFVTA-PNKFEALAAHDALVEAsgaLKTLA- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 245 gmVHLSRFAEDLIFFNTG-EAGFVELS--DRVtSGSSLMPQKKNP---DALELIrgkCGRVQG-----ALTGM------- 306
PRK00485 286 --VSLMKIANDIRWLASGpRCGLGELSlpENE-PGSSIMPGKVNPtqcEALTMV---CAQVMGndaavTFAGSqgnfeln 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 307 MMtlkgLPL-AYNkdMQEDKEGLFDAldtwldCLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADY 373
PRK00485 360 VF----KPViAYN--FLQSIRLLADA------MRSFADHCVVGIEPNEERIKELLERslmlvtalnphiGYDKAAKIAKK 427
|
330
....*....|.
1TJ7_A 374 LVAKGVPFREA 384
PRK00485 428 AHKEGLTLKEA 438
|
|
|
|
|
|
|
-1 |
102353 |
PRK06390 |
PRK06390 |
adenylosuccinate lyase; Provisional |
adenylosuccinate lyase; Provisional |
false |
true |
false |
451 |
4e-10 |
61.08 |
48.34 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 72 RPQQILESDAEDIHSWVEGkLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVM 151
PRK06390 66 RVREIESEIKHDVMALVEA-LSEQCSAGKNYVHFGVTSNDINDTATALQIHDFVSIIKDDIKNLMETLIKLIDEYKDSPM 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 152 PGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRL----DVSPLGCGA-LAGTAYEIdREQLAGWLGFASATRNSl 226
PRK06390 145 MGRTHGQHASPITFGLKFAVYLDEMSRHLDRLTEMGDRAfagkVLGPVGTGAaLGKDALDI-QNRVMEILGIYSEIGST- 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1TJ7_A 227 dSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGfvELSD----RVTSGSSLMPQKKNP 286
PRK06390 223 -QIVNRDRYIEYLSVINGISVTLEKIATEIRNLQRPEID--EVSEyfdeESQVGSSSMPSKVNP 283
|
|
|
|
|
|
|
-1 |
103464 |
PRK08540 |
PRK08540 |
adenylosuccinate lyase; Reviewed |
adenylosuccinate lyase; Reviewed |
false |
true |
false |
449 |
1e-09 |
60.03 |
70.82 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 97 GQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVT----FAHWclay 172
PRK08540 91 GDAGEYVHFGATSNDIIDTATALQLKDALDILEEKLKTLLGVLLDKAEEHKNTVCIGRTHGQHAVPTTygmkFAIW---- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 173 VEMLARDESRLQDALKRLDVSPLgCGALAGTA------YEIDREqLAGWLGFASATRNSldSVSDRDHVLELLSAAAIGM 246
PRK08540 167 ASEIQRHIERLRQLKPRVCVGQM-TGAVGTQAafgekgIEIQKR-VMEILGLGPVDISN--QVIQRDRHAEFMMFLANIA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 247 VHLSRFAEDLIFFNTGEAGFVELS-DRVTSGSSLMPQKKNPDALELIrgkCG--RVQGALtgMMMTLKGLPLAYNKDMQE 323
PRK08540 243 STLDKIGLEIRSLQRTEIGEVEESfGKKQVGSSTMPHKRNPITSEQV---CGlaRVVRSN--VEPALLNNPLWDERDLTN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 324 D--KEGLFDALDTWLD-CLHMAALVLDGIQVKRPRCQE--AAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQ 398
PRK08540 318 SscERVIFPESCVLTDhILNLMIKVLEGLEFNPENIRRnlELTKGLNMAERVMIELAKRGMGRQEAHEIVRQAAMKAHEE 397
|
330
....*....|.
1TJ7_A 399 GKPLEDLPLSE 409
PRK08540 398 GRHLKEVLLEE 408
|
|
|
|
|
|
|
-1 |
102857 |
PRK07380 |
PRK07380 |
adenylosuccinate lyase; Provisional |
adenylosuccinate lyase; Provisional |
false |
true |
false |
431 |
3e-09 |
58.17 |
51.97 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 73 PQQILESDAEDIHSWVE--GKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAV 150
PRK07380 56 PERILEIEAEVRHDVIAflTNVNEYVGDAGRYIHVGMTSSDVLDTGLALQLKASVDLLLEELEKLIQAIRDLAREHKNTV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 151 MPGYTHLQRAQPVTF----AHWcLAyvEMLaRDESRLQDALKRLDVSPLGcGALaGTAYEIDR--EQLA-GWLGFASATR 223
PRK07380 136 MIGRSHAIHGEPITFgfklAGW-LA--ETL-RNRERLERLEEDVAVGQIS-GAM-GTYANTDPevEAITcELLGLKPDTA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 224 NSldSVSDRDHVLELLSAAAIGMVHLSRFA--------EDLI----FFNTGEagfvelsdrvtSGSSLMPQKKNPDALEL 291
PRK07380 210 ST--QVISRDRHAEYVQTLALVGASLERFAteirnlqrTDVLeveeYFAKGQ-----------KGSSAMPHKRNPIRSER 276
|
...
1TJ7_A 292 IRG 294
PRK07380 277 ISG 279
|
|
|
|
|
|
|
-1 |
105640 |
PRK12425 |
PRK12425 |
fumarate hydratase; Provisional |
fumarate hydratase; Provisional |
false |
true |
false |
464 |
5e-07 |
51.13 |
42.89 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 104 HTGRSR--NDQVATDLKLWCKDTV-SELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDE 180
PRK12425 131 HVNRSQssNDCFPTAMHIAAAQAVhEQLLPAIAELSSGLAELSARHMKLVKTGRTHMMDATPITFGQELSAFVAQLDYAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 181 SRLQDALKRldVSPLGCGALA---------GTAYEIDRE--QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHL 249
PRK12425 211 RAIRAALPA--VYELAQGGTAvgtglnapkGFAEAIAAElaALSG-LPFVTAP-NKFAALAGHEPLTSLSGALKTLAVAL 286
|
170 180 190 200
....*....|....*....|....*....|....*....|...
1TJ7_A 250 SRFAEDLIFFNTG-EAGFVELSDRVTS-GSSLMPQKKNPDALE 290
PRK12425 287 MKIANDLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCE 329
|
|
|
|
|
|
|
-1 |
103437 |
PRK08470 |
PRK08470 |
adenylosuccinate lyase; Provisional |
adenylosuccinate lyase; Provisional |
false |
true |
false |
442 |
1e-06 |
49.41 |
47.96 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 96 VGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEM 175
PRK08470 81 LGEESRFVHYGMTSSDCIDTAVALQMKDSLKLIIEDVKNLMEAIKKRALEHKNTLMVGRSHGIHGEPITFGLVLAIWYDE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 176 LARDESRLQDALKRLDVSPLGcGALAGTAYE-IDREQLA-GWLGFASATRNslDSVSDRDHVLELLSAAAIGMVHLSRFA 253
PRK08470 161 IKRHLKLLEHTKEVISVGKIS-GAMGNFAHApLELEELVcEELGLKPAPVS--NQVIQRDRYARLASALALLASSCEKIA 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1TJ7_A 254 EDLIFFNTGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMM 307
PRK08470 238 VAIRHLQRTEVYEAeEYFSPGQKGSSAMPHKRNPVLSENITGLCRVIRSFVTPAL 292
|
|
|
|
|
|
|
-1 |
102911 |
PRK07492 |
PRK07492 |
adenylosuccinate lyase; Provisional |
adenylosuccinate lyase; Provisional |
false |
true |
false |
435 |
3e-04 |
41.51 |
44.83 |
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 92 LIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTvSELLTAN-RQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFA-HWC 169
PRK07492 80 LAEFVGPDARFVHQGMTSSDVLDTCLNVQLVRA-ADLLLADlDRVLAALKKRAFEHKDTVTIGRSHGIHAEPTTFGlKLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1TJ7_A 170 LAYVEMlARDESRLQDALKRLDVSPLGcGALaGTAYEID---REQLAGWLGFASATRNSldSVSDRDHVLELLSA----- 241
PRK07492 159 RFYAEF-SRNRERLVAAREEIATCAIS-GAV-GTFANIDprvEEHVAKKLGLKPEPVST--QVIPRDRHAMFFATlgvia 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1TJ7_A 242 -----AAIGMVHLSRF----AEDliFFNTGEagfvelsdrvtSGSSLMPQKKNP 286
PRK07492 234 ssierLAIEIRHLQRTevleAEE--YFSPGQ-----------KGSSAMPHKRNP 274
|
|
|
|
|
|
|
-1 |