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P04079 (GUAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GMP synthase [glutamine-hydrolyzing]

EC=6.3.5.2
Alternative name(s):
GMP synthetase
Short name=GMPS
Glutamine amidotransferase
Gene names
Name:guaA
Ordered Locus Names:b2507, JW2491
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of GMP from XMP. HAMAP-Rule MF_00344

Catalytic activity

ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP-Rule MF_00344

Enzyme regulation

Inhibited by 2-fluoroinosine 5'-monophosphate (F-IMP) and by N(2)-hydroxyguanosine 5'-monophosphate (N(2)-OH-GMP). Ref.7

Pathway

Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP-Rule MF_00344

Subunit structure

Homodimer.

Induction

Activated by cAMP receptor protein (CRP). Repressed by DnaA. Ref.6 Ref.7 Ref.8

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-909122,EBI-909122

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344
PRO_0000140123

Regions

Domain9 – 207199Glutamine amidotransferase type-1
Domain208 – 400193GMPS ATP-PPase
Nucleotide binding235 – 2417ATP HAMAP-Rule MF_00344

Sites

Active site861Nucleophile
Active site1811
Active site1831

Experimental info

Sequence conflict31E → N AA sequence Ref.1

Secondary structure

.................................................................................... 525
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04079 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: D934786DFF3D694B

FASTA52558,679
        10         20         30         40         50         60 
MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN PSGIILSGGP 

        70         80         90        100        110        120 
ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EASNEREFGY AQVEVVNDSA 

       130        140        150        160        170        180 
LVRGIEDALT ADGKPLLDVW MSHGDKVTAI PSDFITVAST ESCPFAIMAN EEKRFYGVQF 

       190        200        210        220        230        240 
HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS 

       250        260        270        280        290        300 
SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG 

       310        320        330        340        350        360 
ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN 

       370        380        390        400        410        420 
VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY 

       430        440        450        460        470        480 
CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF 

       490        500        510        520 
MTAHWAHLPY DFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12."
Tiedeman A.A., Smith J.M., Zalkin H.
J. Biol. Chem. 260:8676-8679(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase."
Zalkin H., Argos P., Narayana S.V.L., Tiedeman A.A., Smith J.M.
J. Biol. Chem. 260:3350-3354(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN GATASE.
[6]"Regulation of the gua operon of Escherichia coli by the DnaA protein."
Tesfa-Selase F., Drabble W.T.
Mol. Gen. Genet. 231:256-264(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION OF EXPRESSION BY DNAA.
[7]"N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase."
Deras M.L., Chittur S.V., Davisson V.J.
Biochemistry 38:303-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[8]"Regulation of the divergent guaBA and xseA promoters of Escherichia coli by the cyclic AMP receptor protein."
Hutchings M.I., Drabble W.T.
FEMS Microbiol. Lett. 187:115-122(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION OF EXPRESSION BY CRP.
Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
[9]"The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families."
Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L.
Nat. Struct. Biol. 3:74-86(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10101 Genomic DNA. Translation: AAB18619.1.
U00096 Genomic DNA. Translation: AAC75560.1.
AP009048 Genomic DNA. Translation: BAA16394.1.
PIRSYECGU. A24640.
RefSeqNP_417002.1. NC_000913.3.
YP_490735.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPMX-ray2.20A/B/C/D1-525[»]
ProteinModelPortalP04079.
SMRP04079. Positions 3-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9852N.
IntActP04079. 8 interactions.
STRING511145.b2507.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protein family/group databases

MEROPSC26.957.

PTM databases

PhosSiteP0809398.

Proteomic databases

PaxDbP04079.
PRIDEP04079.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75560; AAC75560; b2507.
BAA16394; BAA16394; BAA16394.
GeneID12930651.
947334.
KEGGecj:Y75_p2460.
eco:b2507.
PATRIC32120405. VBIEscCol129921_2605.

Organism-specific databases

EchoBASEEB0415.
EcoGeneEG10420. guaA.

Phylogenomic databases

eggNOGCOG0519.
HOGENOMHOG000223964.
KOK01951.
OMAEIKKEYC.
OrthoDBEOG6JHRJV.
PhylomeDBP04079.
ProtClustDBPRK00074.

Enzyme and pathway databases

BioCycEcoCyc:GMP-SYN-MONOMER.
ECOL316407:JW2491-MONOMER.
MetaCyc:GMP-SYN-MONOMER.
BRENDA6.3.4.1. 2026.
UniPathwayUPA00189; UER00296.

Gene expression databases

GenevestigatorP04079.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00344. GMP_synthase.
InterProIPR017926. GATASE.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR022955. GMP_synthase.
IPR025777. GMPS_ATP_PPase_dom.
IPR022310. NAD/GMP_synthase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04079.
PROP04079.

Entry information

Entry nameGUAA_ECOLI
AccessionPrimary (citable) accession number: P04079
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene