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P04079

- GUAA_ECOLI

UniProt

P04079 - GUAA_ECOLI

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
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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

    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.

    Protein family/group databases

    MEROPSiC26.957.

    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

    Pathology & Biotechi

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN    50
    PSGIILSGGP ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV 100
    EASNEREFGY AQVEVVNDSA LVRGIEDALT ADGKPLLDVW MSHGDKVTAI 150
    PSDFITVAST ESCPFAIMAN EEKRFYGVQF HPEVTHTRQG MRMLERFVRD 200
    ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS SVTAMLLHRA 250
    IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG 300
    ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG 350
    KAHVIKSHHN VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR 400
    HPFPGPGLGV RVLGEVKKEY CDLLRRADAI FIEELRKADL YDKVSQAFTV 450
    FLPVRSVGVM GDGRKYDWVV SLRAVETIDF MTAHWAHLPY DFLGRVSNRI 500
    INEVNGISRV VYDISGKPPA TIEWE 525
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Protein family/group databases

    MEROPSi C26.957.

    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.
    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

    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: October 1, 2014
    This is version 150 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