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Reviewed, UniProtKB/Swiss-Prot P04079 (GUAA_ECOLI)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the synthesis of GMP from XMP. HAMAP MF_00344

Catalytic activity

ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP 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 (glutamine route): step 1/1. HAMAP MF_00344

Subunit structure

Homodimer. HAMAP MF_00344

Induction

Activated by cAMP receptor protein (CRP). Repressed by dnaA. HAMAP MF_00344

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Contains 1 GMP-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

oppAP238431EBI-909122,EBI-1123030

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Domain9 – 207199Glutamine amidotransferase type-1
Domain239 – 401163GMP-binding
Nucleotide binding235 – 2417ATP HAMAP MF_00344

Sites

Active site861Nucleophile HAMAP MF_00344
Active site1811 HAMAP MF_00344
Active site1831 HAMAP MF_00344

Experimental info

Sequence conflict31E → N AA sequence Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04079-1 [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: 3894345] [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: 9205837] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 2982857] [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: 1736096] [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: 9890911] [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: 10856643] [Abstract]
Cited for: REGULATION OF EXPRESSION BY CRP.
Strain: K12 / JM101 / ATCC 33876 / DSM 3948.
[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: 8548458] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases

M10101 Genomic DNA. Translation: AAB18619.1.
U00096 Genomic DNA. Translation: AAC75560.1.
AP009048 Genomic DNA. Translation: BAA16394.1.
PIRSYECGU. A24640.
RefSeqAP_003093.1.
NP_417002.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GPMX-ray2.20A/B/C/D1-525[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9852N.
IntActP04079. 8 interactions.

PTM databases

PhosSiteP04079.

Genome annotation databases

GeneID947334.
GenomeReviewsGene locus JW2491 in contig AP009048_GR.
Gene locus b2507 in contig U00096_GR.
KEGGecj:JW2491.
eco:b2507.

Organism-specific databases

EchoBASEEB0415.
EcoGeneEG10420. guaA.
CMRSearch...

Phylogenomic databases

HOGENOMP04079.
OMAP04079. NEGDMVM.

Enzyme and pathway databases

BioCycEcoCyc:GMP-SYN-MON.
MetaCyc:GMP-SYN-MON.
BRENDA6.3.4.1. 246.

Family and domain databases

HAMAPMF_00344.
[Tree]
InterProIPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR001674. GMP_synth_C.
IPR004739. GMP_synth_N.
IPR014729. Rossmann-like_a/b/a_fold.
IPR018318. tRNA_MeTrfase-like.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF03054. tRNA_Me_trans. 1 hit.
[Graphical view]
PRINTSPR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.
TIGRFAMsTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.

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: June 16, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents