GMP synthase [glutamine-hydrolyzing] - Escherichia coli (strain K12)

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P04079 (GUAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the synthesis of GMP from XMP. HAMAP-Rule MF_00344
Catalytic activity	ATP + xanthosine 5'-phosphate + 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.

Ontologies

Keywords
Biological process	GMP biosynthesis Purine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP GMP synthase (glutamine-hydrolyzing) activity Inferred from direct assay Ref.7. Source: EcoCyc GMP synthase activity Inferred from direct assay PubMed 17103135. Source: EcoCyc pyrophosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-909122,EBI-909122

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 525

525

GMP synthase [glutamine-hydrolyzing] HAMAP-Rule MF_00344

PRO_0000140123

Regions

Domain

9 – 207

199

Glutamine amidotransferase type-1

Domain

208 – 400

193

GMPS ATP-PPase

Nucleotide binding

235 – 241

ATP HAMAP-Rule MF_00344

Sites

Active site

Nucleophile

Active site

181

Active site

183

Experimental info

Sequence conflict

E → N AA sequence Ref.1

Secondary structure

525

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04079 [UniParc].

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

FASTA

525

58,679

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

SYECGU. A24640.

RefSeq

NP_417002.1. NC_000913.2.
YP_490735.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GPM	X-ray	2.20	A/B/C/D	1-525	[»]

ProteinModelPortal

P04079.

SMR

P04079. Positions 3-525.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9852N.

IntAct

P04079. 8 interactions.

STRING

511145.b2507.

Protein family/group databases

MEROPS

C26.957.

PTM databases

PhosSite

P0809398.

Proteomic databases

PaxDb

P04079.

PRIDE

P04079.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75560; AAC75560; b2507.
BAA16394; BAA16394; BAA16394.

GeneID

12930651.
947334.

KEGG

ecj:Y75_p2460.
eco:b2507.

PATRIC

32120405. VBIEscCol129921_2605.

Organism-specific databases

EchoBASE

EB0415.

EcoGene

EG10420. guaA.

Phylogenomic databases

eggNOG

COG0519.

HOGENOM

HOG000223964.

K01951.

OMA

YDYVVAL.

ProtClustDB

PRK00074.

Enzyme and pathway databases

BioCyc

EcoCyc:GMP-SYN-MONOMER.
ECOL316407:JW2491-MONOMER.
MetaCyc:GMP-SYN-MONOMER.

BRENDA

6.3.4.1. 2026.

UniPathway

UPA00189; UER00296.

Gene expression databases

Genevestigator

P04079.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00344. GMP_synthase.

InterPro

IPR017926. GATASE_1.
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]

Pfam

PF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P04079.

Entry information

Entry name

GUAA_ECOLI

Accession

Primary (citable) accession number: P04079

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents