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P04079

- GUAA_ECOLI

UniProt

P04079 - GUAA_ECOLI

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Protein

GMP synthase [glutamine-hydrolyzing]

Gene

guaA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of GMP from XMP.

Catalytic activityi

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

Enzyme regulationi

Inhibited by 2-fluoroinosine 5'-monophosphate (F-IMP) and by N(2)-hydroxyguanosine 5'-monophosphate (N(2)-OH-GMP).1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Nucleophile
Active sitei181 – 1811
Active sitei183 – 1831

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi235 – 2417ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. GMP synthase (glutamine-hydrolyzing) activity Source: EcoCyc
  3. GMP synthase activity Source: EcoCyc
  4. identical protein binding Source: IntAct
  5. pyrophosphatase activity Source: InterPro

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB-HAMAP
  2. GMP biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

GMP biosynthesis, Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GMP-SYN-MONOMER.
ECOL316407:JW2491-MONOMER.
MetaCyc:GMP-SYN-MONOMER.
BRENDAi6.3.4.1. 2026.
UniPathwayiUPA00189; UER00296.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP synthase [glutamine-hydrolyzing] (EC:6.3.5.2)
Alternative name(s):
GMP synthetase
Short name:
GMPS
Glutamine amidotransferase
Gene namesi
Name:guaA
Ordered Locus Names:b2507, JW2491
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10420. guaA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525GMP synthase [glutamine-hydrolyzing]PRO_0000140123Add
BLAST

Proteomic databases

PaxDbiP04079.
PRIDEiP04079.

PTM databases

PhosSiteiP0809398.

Expressioni

Inductioni

Activated by cAMP receptor protein (CRP). Repressed by DnaA.

Gene expression databases

GenevestigatoriP04079.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909122,EBI-909122

Protein-protein interaction databases

DIPiDIP-9852N.
IntActiP04079. 8 interactions.
STRINGi511145.b2507.

Structurei

Secondary structure

1
525
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Helixi20 – 2910Combined sources
Beta strandi33 – 397Combined sources
Helixi43 – 497Combined sources
Beta strandi52 – 565Combined sources
Helixi73 – 764Combined sources
Beta strandi78 – 803Combined sources
Beta strandi82 – 854Combined sources
Helixi87 – 959Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi107 – 1159Combined sources
Turni120 – 1245Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi145 – 1495Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi166 – 1705Combined sources
Turni171 – 1744Combined sources
Beta strandi175 – 1806Combined sources
Helixi190 – 19910Combined sources
Helixi210 – 22516Combined sources
Beta strandi229 – 2335Combined sources
Helixi238 – 25114Combined sources
Helixi252 – 2543Combined sources
Beta strandi255 – 2617Combined sources
Helixi269 – 2779Combined sources
Turni278 – 2814Combined sources
Beta strandi285 – 2895Combined sources
Helixi291 – 2988Combined sources
Helixi304 – 32522Combined sources
Beta strandi326 – 3338Combined sources
Helixi338 – 3436Combined sources
Beta strandi371 – 3733Combined sources
Turni375 – 3784Combined sources
Helixi381 – 39010Combined sources
Helixi395 – 3984Combined sources
Helixi407 – 4104Combined sources
Helixi418 – 43720Combined sources
Helixi441 – 4433Combined sources
Beta strandi444 – 45714Combined sources
Turni460 – 4623Combined sources
Beta strandi465 – 47915Combined sources
Beta strandi482 – 4854Combined sources
Helixi490 – 50314Combined sources
Beta strandi507 – 5137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPMX-ray2.20A/B/C/D1-525[»]
ProteinModelPortaliP04079.
SMRiP04079. Positions 3-525.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04079.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 207199Glutamine amidotransferase type-1Add
BLAST
Domaini208 – 400193GMPS ATP-PPaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0519.
HOGENOMiHOG000223964.
InParanoidiP04079.
KOiK01951.
OMAiKIYGLQF.
OrthoDBiEOG6JHRJV.
PhylomeDBiP04079.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00344. GMP_synthase.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. 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]
PfamiPF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04079-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN
60 70 80 90 100
PSGIILSGGP ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV
110 120 130 140 150
EASNEREFGY AQVEVVNDSA LVRGIEDALT ADGKPLLDVW MSHGDKVTAI
160 170 180 190 200
PSDFITVAST ESCPFAIMAN EEKRFYGVQF HPEVTHTRQG MRMLERFVRD
210 220 230 240 250
ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS SVTAMLLHRA
260 270 280 290 300
IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG
310 320 330 340 350
ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG
360 370 380 390 400
KAHVIKSHHN VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR
410 420 430 440 450
HPFPGPGLGV RVLGEVKKEY CDLLRRADAI FIEELRKADL YDKVSQAFTV
460 470 480 490 500
FLPVRSVGVM GDGRKYDWVV SLRAVETIDF MTAHWAHLPY DFLGRVSNRI
510 520
INEVNGISRV VYDISGKPPA TIEWE
Length:525
Mass (Da):58,679
Last modified:January 1, 1988 - v1
Checksum:iD934786DFF3D694B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31E → N AA sequence (PubMed:3894345)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10101 Genomic DNA. Translation: AAB18619.1.
U00096 Genomic DNA. Translation: AAC75560.1.
AP009048 Genomic DNA. Translation: BAA16394.1.
PIRiA24640. SYECGU.
RefSeqiNP_417002.1. NC_000913.3.
YP_490735.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75560; AAC75560; b2507.
BAA16394; BAA16394; BAA16394.
GeneIDi12930651.
947334.
KEGGiecj:Y75_p2460.
eco:b2507.
PATRICi32120405. VBIEscCol129921_2605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10101 Genomic DNA. Translation: AAB18619.1 .
U00096 Genomic DNA. Translation: AAC75560.1 .
AP009048 Genomic DNA. Translation: BAA16394.1 .
PIRi A24640. SYECGU.
RefSeqi NP_417002.1. NC_000913.3.
YP_490735.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GPM X-ray 2.20 A/B/C/D 1-525 [» ]
ProteinModelPortali P04079.
SMRi P04079. Positions 3-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9852N.
IntActi P04079. 8 interactions.
STRINGi 511145.b2507.

PTM databases

PhosSitei P0809398.

Proteomic databases

PaxDbi P04079.
PRIDEi P04079.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75560 ; AAC75560 ; b2507 .
BAA16394 ; BAA16394 ; BAA16394 .
GeneIDi 12930651.
947334.
KEGGi ecj:Y75_p2460.
eco:b2507.
PATRICi 32120405. VBIEscCol129921_2605.

Organism-specific databases

EchoBASEi EB0415.
EcoGenei EG10420. guaA.

Phylogenomic databases

eggNOGi COG0519.
HOGENOMi HOG000223964.
InParanoidi P04079.
KOi K01951.
OMAi KIYGLQF.
OrthoDBi EOG6JHRJV.
PhylomeDBi P04079.

Enzyme and pathway databases

UniPathwayi UPA00189 ; UER00296 .
BioCyci EcoCyc:GMP-SYN-MONOMER.
ECOL316407:JW2491-MONOMER.
MetaCyc:GMP-SYN-MONOMER.
BRENDAi 6.3.4.1. 2026.

Miscellaneous databases

EvolutionaryTracei P04079.
PROi P04079.

Gene expression databases

Genevestigatori P04079.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.40.50.880. 1 hit.
HAMAPi MF_00344. GMP_synthase.
InterProi IPR029062. Class_I_gatase-like.
IPR017926. 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 ]
Pfami PF00117. GATase. 1 hit.
PF00958. GMP_synt_C. 1 hit.
PF02540. NAD_synthase. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR00884. guaA_Cterm. 1 hit.
TIGR00888. guaA_Nterm. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
PS51553. GMPS_ATP_PPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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).

Entry informationi

Entry nameiGUAA_ECOLI
AccessioniPrimary (citable) accession number: P04079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 1, 1988
Last modified: November 26, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3