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Streptococcus sanguinis Search Results

Record: 1 of 1  
MiniMap IGR991 IGR990 IGR992 IGR988 IGR994 IGR993 IGR989 IGR987 mutX, - SSA_1236 pyrE, - SSA_1240 ung, - SSA_1237 pyrF, - SSA_1241 SSA_1238 pyrC, - SSA_1235 SSA_1239 parE, - SSA_1232 SSA_1234 SSA_1233 mutX, - SSA_1236 pyrE, - SSA_1240 ung, - SSA_1237 pyrF, - SSA_1241 SSA_1238 pyrC, - SSA_1235 SSA_1239 parE, - SSA_1232 SSA_1234 SSA_1233 mutX, - SSA_1236 ung, - SSA_1237 pyrF, - SSA_1241 SSA_1238 pyrC, - SSA_1235 SSA_1239 parE, - SSA_1232 SSA_1234 pyrE, - SSA_1240 SSA_1233


Gene ID:SSA_1235

DNA Molecule Name:
1  

GenBank ID:
125497972

Gene Name:
pyrC  

Species Definition:
dihydroorotase

GenBank Definition:
Dihydroorotase, putative

Cellular Location:
Cytoplasm, Extracellular [Evidence]

Gene Start:
1261314

Gene Stop:
1260052

Gene Length:
1263

Molecular Weight*:
45064

pI*:
5.61

Net Charge*:
-15.48

EC:
3.5.2.3  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Nucleotide and nucleoside interconversions  

Gene Ontology:
Molecular function
  GO:0016787    hydrolase activity
  GO:0016812    hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides


Pathway: pathway table

Primary Evidence:
Xu P, Alves JM, Kitten T, Brown A, Chen Z, Ozaki LS, Manque P, Ge X, Serrano MG, Puiu D,
Hendricks S, Wang Y, Chaplin MD, Akan D, Paik S, Peterson DL, Macrina FL, Buck GA.
Genome of the Opportunistic Pathogen Streptococcus sanguinis.
J Bacteriol. 2007 Apr; 189(8):3166-75.
PMID: 17277061


Comment:


View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search


Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|125718055|ref|YP_001035188.1|  Dihydroorotase, putative [...   786   0.0  
 gi|157076146|gb|ABV10829.1|  dihydroorotase [Streptococcus g...   756   0.0  
 gi|24379638|ref|NP_721593.1|  dihydroorotase [Streptococcus ...   643   0.0  
 gi|55821079|ref|YP_139521.1|  dihydroorotase [Streptococcus ...   639   0.0  
 gi|116627822|ref|YP_820441.1|  Dihydroorotase [Streptococcus...   639   0.0  
 gi|148989199|ref|ZP_01820589.1|  dihydroorotase [Streptococc...   634   e-180
 gi|149025521|ref|ZP_01836454.1|  dihydroorotase [Streptococc...   632   e-179
 gi|15903097|ref|NP_358647.1|  dihydroorotase [Streptococcus ...   631   e-179
 gi|148994517|ref|ZP_01823697.1|  dihydroorotase [Streptococc...   630   e-179
 gi|15901032|ref|NP_345636.1|  dihydroorotase [Streptococcus ...   630   e-179


InterPro Summary:  InterProScan

InterPro
IPR002195
Domain
Dihydroorotase
PS00482 [56-64]T 8e-5 PS00482 DIHYDROOROTASE_1 DIHYDROOROTASE_1
PS00483 [300-311]T 8e-5 PS00483 DIHYDROOROTASE_2 DIHYDROOROTASE_2
InterPro
IPR004722
Domain
Dihydroorotase multifunctional complex type
TIGR00857 [14-421]T 1.7e-105 TIGR00857 pyrC_multi: dihydroorotase, multifunctional pyrC_multi: dihydroorotase, multifunctional
InterPro
IPR006680
Domain
Amidohydrolase 1
PF01979 [49-379]T 5.6e-18 PF01979 Amidohydro_1 Amidohydro_1
noIPR
unintegrated
unintegrated
G3DSA:3.20.20.140 [53-405]T 4.3e-93 G3DSA:3.20.20.140 no description no description
PTHR11647 [42-420]T 2.5e-120 PTHR11647 AMINOHYDROLASE AMINOHYDROLASE
PTHR11647:SF2 [42-420]T 2.5e-120 PTHR11647:SF2 DIHYDROOROTASE DIHYDROOROTASE


COGS Summary:  COGS Search
No hits to the COGs database.
Blocks Summary:  Blocks Search
***** IPB005847 (Dihydroorotase region) with a combined E-value of 1e-29.
    IPB005847A    3-32
    IPB005847B    55-89
    IPB005847F    217-265
    IPB005847G    308-334
    IPB005847H    361-380
    IPB005847I    396-421
***** IPB002195 (Dihydroorotase) with a combined E-value of 2.8e-19.
    IPB002195A    82-96
    IPB002195B    249-265
    IPB002195C    299-311
***** IPB012855 (D-aminoacylase, C-terminal) with a combined E-value of 3.6e-10.
    IPB012855A    0-32
    IPB012855B    43-54
    IPB012855I    364-406
***** IPB013108 (Amidohydrolase 3) with a combined E-value of 5e-06.
    IPB013108A    43-62


 ProDom Summary:  Protein Domain Search
Residues 1-110 are 54% similar to a (SUBUNIT PYRC_apos; ASPARTATE TRANSCARBAMOYLASE) protein domain (PDA188T4 which is seen in Q9A5K3_CAUCR.

Residues 1-42 are 88% similar to a (DIHYDROOROTASE HYDROLASE TYPE ZINC DIHYDROOROTASE PYRIMIDINE METAL-BINDING DHOASE BIOSYNTHESIS MULTIFUNCTIONAL) protein domain (PDA0H6A3 which is seen in Q8DTV9_STRMU.

Residues 1-163 are 52% similar to a (DIHYDROOROTASE) protein domain (PDA1D3Z7 which is seen in Q7NEQ6_GLOVI.

Residues 7-65 are 68% similar to a (DIHYDROOROTASE HYDROLASE CHAIN TYPE NON-CATALYTIC DIHYDROOROTASE-LIKE ASPARTATE MULTIFUNCTIONAL COMPLEX CARBAMOYLTRANSFERASE) protein domain (PD701049 which is seen in Q87V98_PSESM.

Residues 43-68 are 96% similar to a (DIHYDROOROTASE HYDROLASE PYRIMIDINE BIOSYNTHESIS ZINC METAL-BINDING DHOASE TYPE DIHYDROOROTASE MULTIFUNCTIONAL) protein domain (PD345283 which is seen in PYRC_LACLA.

Residues 65-360 are similar to a (HYDROLASE DIHYDROOROTASE ZINC PYRIMIDINE BIOSYNTHESIS METAL-BINDING DHOASE DIHYDROPYRIMIDINASE COLLAPSIN MEDIATOR) protein domain (PD001085 which is seen in Q8DTV9_STRMU.

Residues 225-420 are 45% similar to a (P32375 ALLANTOINASE SINGLETON DAL1 SACCHAROMYCES CEREVISIAE YIR027C) protein domain (PD946212 which is seen in Q6CUK0_EEEEE.

Residues 338-383 are 80% similar to a (ZINC PYRIMIDINE HYDROLASE METAL-BINDING DHOASE DIHYDROOROTASE BIOSYNTHESIS) protein domain (PDA198O9 which is seen in PYRC_LACLA.


Paralogs:  Local Blast Search
SSA_1235 has no significant similarity (blastp p-value < 1e-6) to any other gene in this genome.

Pfam Summary:  Pfam Search
Residues 49 to 379 (E_value = 6e-18) place SSA_1235 in the Amidohydro_1 family which is described as Amidohydrolase family.


 Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
75  
91

Top PDB Hits:
57% similar to PDB:1XRF The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex aeolicus at 1.7 A resolution (E_value = 8.9E_79);
57% similar to PDB:1XRT The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex Aeolicus at 1.7 A Resolution (E_value = 8.9E_79);
42% similar to PDB:2GWN The structure of putative dihydroorotase from Porphyromonas gingivalis. (E_value = 8.1E_24);
42% similar to PDB:1GKR L-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM ARTHROBACTER AURESCENS (E_value = 1.2E_22);
42% similar to PDB:1YNY Molecular Structure of D-Hydantoinase from a Bacillus sp. AR9: Evidence for mercury inhibition (E_value = 4.5E_22);

Gene Protein Sequence:
LLIKNGRVMDPKTGFDQIADLLVEGKKIIKIGQDLQVKDAKVIDASGLVV
APGLVDIHVHFREPGQTHKEDIHTGALAAAAGGFTTVVMMANTNPAISTV
ETLKEVLESASRENIHIKSVATITENFDGQHLTDFQGLLAAGAVGFSDDG
IPLTNAGIVRQALVEARKNDTFISLHEEDPNLNGILGFNEHIAKEHFHIC
GATGVAEYSMIARDVMIAFDAKAHVHIQHLSKSESVKVVEFAQMLGAQVT
AEAAPQHFSKTEALLLTKGSNAKMNPPLRLESDRLSVIEGLKSGIISVIA
TDHAPHHADEKNVADITQAPSGMTGLETSLSLGLTYLVEAGHLSLMELLE
KMTFNPAQLYGFDAGFIAQDGPADLTIFDPEADRLVTDHFASKAANSPFV
GEKLKGQVKFTICDGEVVFKG

Gene Nucleotide Sequence:  Sequence Viewer
ctattaatcaaaaacggacgagttatggatcctaagactggttttgacca
aattgccgacctcttggttgaggggaagaaaattattaaaattggtcaag
atttacaggtgaaagatgcaaaagttattgatgccagtggtttggttgtg
gctcctggtttggtggatatacatgtgcatttccgggagccgggccagac
tcataaggaagatattcatacgggggctttggcagcagcagcaggtggct
ttacgactgttgttatgatggccaataccaatccggccatctctacagtt
gaaaccctgaaggaagtactggagtcggctagtcgtgaaaatatccatat
caagtcggtcgcgacgatcacagagaattttgatgggcagcatctgacag
atttccaaggtctcttggcagctggtgcagtaggtttttctgatgacggt
attccattgaccaacgctggcattgtccgccaagccctcgtagaagcacg
taaaaatgacacctttatcagcttgcacgaggaagatcccaatctcaacg
gcatactcggtttcaatgagcatatcgctaaagagcattttcatatctgt
ggcgcgacaggtgtggcagaatatagcatgattgctcgcgatgtcatgat
tgcttttgatgcgaaggctcatgtgcatatccagcatttgtccaagtctg
agagtgtaaaggtggtggaattcgctcagatgctaggcgctcaagtcacc
gctgaagcagcacctcagcacttctctaagacagaagctctgctattgac
caagggcagcaatgctaagatgaatccgcctctgcgcttagaatcggatc
gtctgtcggttattgaggggctcaaatctggtatcatttctgtcattgcg
acggaccatgctccacatcatgctgacgagaaaaatgtagccgatatcac
tcaggcgccttctggtatgactgggcttgagacttcgctttctctgggac
tgacctacttggtagaggctggtcatctgagcttgatggagcttttggag
aaaatgacatttaatccagctcagttgtatggttttgatgctggattcat
cgctcaggatggtcctgctgatttgacaatatttgatccagaagcagata
gacttgtgactgaccactttgcctccaaggcagccaattcaccttttgtt
ggtgaaaagcttaaaggccaagtgaagtttactatctgtgatggggaagt
tgtctttaaagga

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