Basic Search | Intermediate Search | Gene Image Map |  Home

Porphyromonas gingivalis Search Results

Record: 1 of 1  
MiniMap IGR0445 IGR0448 IGR0451 IGR0449 IGR0454 IGR0453 IGR0446 IGR0447 IGR0450 IGR0452 PG0529 PG0530 guaA, - PG0531 PG0527.1 rl31, - PG0534 ISPg5, - PG0532 PG0527 ISPg5, - PG0533 ftsZ, - PG0526 htrA, - PG0535 PG0529 PG0530 guaA, - PG0531 PG0527.1 rl31, - PG0534 ISPg5, - PG0532 PG0527 ISPg5, - PG0533 ftsZ, - PG0526 htrA, - PG0535 Type: IS element, Name: ISPg5 - 8 Type: tandem, Name: tan38 - 246 Type: tandem, Name: tan39 - 247 PG0529 PG0530 guaA, - PG0531 rl31, - PG0534 ISPg5, - PG0532 PG0527 ISPg5, - PG0533 ftsZ, - PG0526 htrA, - PG0535 PG0527.1


LANL Gene ID: PG0531

GenBank Locus Tag: PG0589

DNA Molecule Name:
1  

GenBank ID:
34540397

Gene Name:
guaA  

Definition:
GMP synthase

Cellular Location:
Cytoplasm [Evidence]

Gene Start:
647799

Gene Stop:
646282

Gene Length:
1518

Molecular Weight*:
56698

pI*:
6.00

Net Charge*:
-8.05

EC:
6.3.5.2  

Functional Class:
Purines, pyrimidines, nucleosides and nucleotides; Purine ribonucleotide biosynthesis  

Gene Ontology:
Biological process
  GO:0009058    biosynthetic process
  GO:0008033    tRNA processing
  GO:0006541    glutamine metabolic process
  GO:0006177    GMP biosynthetic process
  GO:0006164    purine nucleotide biosynthetic process

Cellular component
  GO:0005737    cytoplasm

Molecular function
  GO:0005524    ATP binding
  GO:0004808    tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity
  GO:0003922    GMP synthase (glutamine-hydrolyzing) activity
  GO:0003824    catalytic activity


Pathway: pathway table
Glutamate metabolism
Purine metabolism

Comment:
TIGR ID: PG0589

Proteomic Data Search
View in HOMD Genome Viewer

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to GMP synthase protein,
residues 4-506 are 53% similar to (AE000337) GMP synthetase (glutamine-hydrolyzing) of Escherichia coli, residues 3-506 are 55% similar to (AE004052) glutamine amidotransferase of Xylella fastidiosa, residues 5-506 are 53% similar to (AE002027) GMP synthase of Deinococcus radiodurans.

This sequence is similar to BT4265.

Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|34540397|ref|NP_904876.1|  bifunctional GMP synthase/glut...  1046   0.0  
 gi|154493620|ref|ZP_02032940.1|  hypothetical protein PARMER...   854   0.0  
 gi|150008447|ref|YP_001303190.1|  glutaminne-hydrolyzing GMP...   848   0.0  
 gi|53712261|ref|YP_098253.1|  bifunctional GMP synthase/glut...   803   0.0  
 gi|29349673|ref|NP_813176.1|  bifunctional GMP synthase/glut...   796   0.0  
 gi|156107494|gb|EDO09239.1|  hypothetical protein BACOVA_050...   792   0.0  
 gi|153807599|ref|ZP_01960267.1|  hypothetical protein BACCAC...   791   0.0  
 gi|150006078|ref|YP_001300822.1|  glutaminne-hydrolyzing GMP...   780   0.0  
 gi|156859184|gb|EDO52615.1|  hypothetical protein BACUNI_034...   750   0.0  
 gi|110637346|ref|YP_677553.1|  GMP synthetase (glutamine-hyd...   700   0.0


InterPro Summary:  InterProScan

InterPro
IPR000991
Domain
Glutamine amidotransferase class-I
PF00117 [6-187]T 6.8999844819926704E-37 PF00117 GATase GATase
InterPro
IPR001674
Domain
GMP synthase, C-terminal
PF00958 [413-505]T 1.9000069431526998E-45 PF00958 GMP_synt_C GMP_synt_C
TIGR00884 [197-506]T 0.0 TIGR00884 guaA_Cterm guaA_Cterm
InterPro
IPR004506
Family
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase
PF03054 [213-235]T 3.60000038700736E-5 PF03054 tRNA_Me_trans tRNA_Me_trans
InterPro
IPR004739
Domain
GMP synthase, N-terminal
TIGR00888 [5-190]T 2.6853016927105897E-67 TIGR00888 guaA_Nterm guaA_Nterm
InterPro
IPR006220
Domain
Anthranilate synthase component II/delta crystallin
PR00097 [74-85]T 2.5E-6 PR00097 ANTSNTHASEII[163-176]T 2.5E-6 PR00097 ANTSNTHASEII ANTSNTHASEII
InterPro
IPR011702
Domain
Glutamine amidotransferase superfamily
PR00096 [47-56]T 2.2E-7 PR00096 GATASE[74-85]T 2.2E-7 PR00096 GATASE[163-176]T 2.2E-7 PR00096 GATASE GATASE
InterPro
IPR012998
Active_site
Glutamine amidotransferase, class I, active site
PS00442 [74-85]T 0.0 PS00442 GATASE_TYPE_I GATASE_TYPE_I
InterPro
IPR014729
Domain
Rossmann-like alpha/beta/alpha sandwich fold
G3DSA:3.40.50.620 [192-381]T 7.199963955439732E-75 G3DSA:3.40.50.620 Rossmann-like_a/b/a_fold Rossmann-like_a/b/a_fold
noIPR
unintegrated
unintegrated
G3DSA:3.30.300.10 [398-506]T 4.9000102778240796E-45 G3DSA:3.30.300.10 G3DSA:3.30.300.10 G3DSA:3.30.300.10
G3DSA:3.40.50.880 [4-191]T 1.49999648196318E-52 G3DSA:3.40.50.880 G3DSA:3.40.50.880 G3DSA:3.40.50.880
PTHR11922 [4-506]T 0.0 PTHR11922 PTHR11922 PTHR11922
PTHR11922:SF2 [4-506]T 0.0 PTHR11922:SF2 PTHR11922:SF2 PTHR11922:SF2
SSF52317 [4-225]T 1.1999999999999999E-54 SSF52317 SSF52317 SSF52317
SSF52402 [178-428]T 5.799999999999999E-56 SSF52402 SSF52402 SSF52402


COGS Summary:  COGS Search
BeTs to 14 clades of COG0519
COG name: GMP synthase - PP-ATPase domain
Functional Class: F
The phylogenetic pattern of COG0519 is amtkyqvcebrhuj--o--n-
Number of proteins in this genome belonging to this COG is 1
Blocks Summary:  Blocks Search
***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 4.5e-07.
    IPB000991A    74-83
    IPB000991B    160-171


 ProDom Summary:  Protein Domain Search
Residues 46-184 are 47% similar to a (SYNTHASE GLUTAMINE BIOSYNTHESIS AMIDOTRANSFERASE) protein domain (PD000306 which is seen in GUAA_BACSU.

Residues 302-506 are 64% similar to a (GMP SYNTHASE SYNTHETASE) protein domain (PD003340 which is seen in GUAA_ECOLI.

Residues 212-300 are 67% similar to a (PROTEIN SYNTHETASE LIGASE BIOSYNTHESIS PROBABLE) protein domain (PD000352 which is seen in O85192_BBBBB.


Paralogs:  Local Blast Search
No paralogs found in P.gingivalis.

Pfam Summary:  Pfam Search
Residues 6 to 187 (E-value = 3.5e-40) place PG0531 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)
Residues 386 to 505 (E-value = 2.3e-63) place PG0531 in the GMP_synt_C family which is described as GMP synthase C terminal domain (PF00958)

 Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
215  
231
non-globular  
323  
399

Top PDB Hits:
-71% similar to PDB:1GPM ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE (E_value = 6.5E_156);
-73% similar to PDB:2DPL Crystal Structure of the GMP synthase from Pyrococcus horikoshii OT3 (E_value = 2.1E_82);
-49% similar to PDB:2D7J Crystal Structure Analysis of Glutamine Amidotransferase from Pyrococcus horikoshii OT3 (E_value = 9.5E_22);
-49% similar to PDB:1WL8 Crystal structure of PH1346 protein from Pyrococcus horikoshii (E_value = 6.1E_21);
-48% similar to PDB:2A9V Crystal structure of (np_394403.1) from THERMOPLASMA ACIDOPHILUM at 2.45 A resolution (E_value = 4.0E_20);

Gene Protein Sequence:
MLEKLIILDFGSQTTQLIARRIRELNTYCEVYPYNKLPEDLSGVRGIILS
GSPYSVYDSKAFRIELSELRGKLPLLGICYGAQSLVHQAGGKVEPCDSRE
YGRTHLTLRQPDDALLTGLQSGTTVWMSHGDTITSLPEGFEVIAGTEDVP
NAAFRIRGEKTWGVQFHPEIYHSEEGTKLLGNFLDICGMKRDWTPASFIE
ATVQELRERLGDDKVILALSGGVDSSVVAVLLNKAIGRNLTCIFVDHGLL
RKGEFERVLQDYEHLGLNVIGVNAKEKFFAALSGVTDPEQKRKIIGRGFI
EVFDEEARKLKDIKWLGQGTIYPDVIESLSITGMVIKSHHNVGGLPERMN
LRLVEPLRMLFKDEVRRVGLELGMMPHLIHRHPFPGPGLGIRILGEITEE
KATILQNADDIYMSLMREWGLYDQVWQAGAILLPVRSVGVMGDERTYEYT
VALRAVTSMDAMSADWVHLPYDFLAKVSNEIINKVRGVNRVVYDISSKPP
STIEWE

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTGGAAAAGCTCATTATTCTGGATTTCGGTTCTCAAACCACACAGCT
CATCGCCAGACGAATTCGCGAGCTGAACACCTACTGCGAGGTTTATCCCT
ACAACAAACTGCCGGAAGACCTCTCAGGAGTGCGAGGCATCATCCTGTCG
GGGAGCCCTTATTCCGTGTATGACAGCAAGGCCTTTCGTATCGAACTGAG
CGAATTACGGGGCAAGTTGCCTCTCTTGGGTATCTGCTACGGTGCACAGA
GCCTTGTCCATCAAGCCGGTGGCAAAGTAGAGCCGTGCGACAGTCGCGAA
TACGGGCGAACACATCTGACCCTCCGGCAGCCTGATGATGCACTGCTGAC
AGGCCTGCAATCCGGCACTACGGTATGGATGTCCCACGGCGATACCATTA
CGTCATTGCCTGAAGGATTCGAGGTCATAGCAGGTACCGAGGATGTACCC
AATGCAGCATTTCGCATCCGAGGGGAGAAAACGTGGGGCGTACAGTTCCA
TCCCGAGATCTACCACTCGGAAGAAGGTACCAAACTGCTTGGCAACTTCC
TCGATATATGCGGTATGAAGCGTGATTGGACTCCGGCTTCTTTCATCGAA
GCGACTGTGCAGGAACTTCGCGAACGCTTAGGTGATGACAAGGTGATCCT
GGCACTCTCCGGAGGTGTGGACAGTTCGGTGGTGGCGGTGCTTCTGAACA
AAGCTATCGGCCGCAACCTGACTTGTATATTCGTCGATCACGGCTTGCTG
CGTAAGGGCGAATTCGAGCGCGTACTTCAGGACTACGAGCACTTGGGTCT
CAATGTAATCGGGGTGAATGCAAAAGAAAAATTCTTCGCAGCCCTTAGCG
GCGTTACCGATCCCGAGCAAAAACGGAAGATTATCGGTCGCGGCTTCATC
GAAGTGTTCGACGAAGAAGCCCGGAAGCTGAAAGATATCAAATGGCTTGG
TCAGGGCACGATCTACCCCGATGTCATTGAAAGTCTGAGTATCACCGGTA
TGGTGATCAAGAGTCACCACAATGTGGGAGGACTGCCCGAGCGGATGAAT
CTCCGCCTCGTGGAACCGCTCCGTATGCTCTTCAAGGACGAAGTCCGTCG
CGTGGGACTCGAGCTCGGCATGATGCCGCACCTGATCCATCGCCATCCTT
TCCCCGGTCCCGGTCTCGGCATCCGTATTCTCGGAGAGATCACGGAAGAG
AAAGCTACCATCTTGCAGAACGCCGATGACATCTATATGAGCCTTATGCG
CGAGTGGGGGCTGTATGATCAGGTGTGGCAGGCCGGAGCCATCCTGCTGC
CGGTTCGGTCCGTAGGCGTAATGGGCGACGAGCGTACCTACGAATACACC
GTGGCACTGCGTGCCGTGACTTCTATGGATGCCATGAGTGCCGATTGGGT
GCATTTGCCGTATGATTTTCTGGCCAAGGTGTCGAACGAAATAATCAATA
AAGTGCGTGGCGTAAACCGCGTAGTCTACGACATCTCCTCCAAACCCCCC
AGCACAATCGAATGGGAA

Los Alamos National Laboratory • Est 1943

Operated by Los Alamos National Security, LLC for the U.S. Department of Energy's National Nuclear Security Administration
Inside | © Copyright 2006 LANS LLC All rights reserved | Disclaimer/Privacy