ID   GUAA_ECOLI              Reviewed;         525 AA.
AC   P04079;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2 {ECO:0000269|PubMed:9890911};
DE   AltName: Full=GMP synthetase;
DE            Short=GMPS;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=b2507, JW2491;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-17.
RX   PubMed=3894345; DOI=10.1016/s0021-9258(17)39400-0;
RA   Tiedeman A.A., Smith J.M., Zalkin H.;
RT   "Nucleotide sequence of the guaA gene encoding GMP synthetase of
RT   Escherichia coli K12.";
RL   J. Biol. Chem. 260:8676-8679(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   DOMAIN GATASE.
RX   PubMed=2982857; DOI=10.1016/s0021-9258(19)83627-x;
RA   Zalkin H., Argos P., Narayana S.V.L., Tiedeman A.A., Smith J.M.;
RT   "Identification of a trpG-related glutamine amide transfer domain in
RT   Escherichia coli GMP synthetase.";
RL   J. Biol. Chem. 260:3350-3354(1985).
RN   [6]
RP   REGULATION OF EXPRESSION BY DNAA.
RX   PubMed=1736096; DOI=10.1007/bf00279799;
RA   Tesfa-Selase F., Drabble W.T.;
RT   "Regulation of the gua operon of Escherichia coli by the DnaA protein.";
RL   Mol. Gen. Genet. 231:256-264(1992).
RN   [7]
RP   ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX   PubMed=9890911; DOI=10.1021/bi981980r;
RA   Deras M.L., Chittur S.V., Davisson V.J.;
RT   "N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of
RT   Escherichia coli guanosine monophosphate synthetase.";
RL   Biochemistry 38:303-310(1999).
RN   [8]
RP   REGULATION OF EXPRESSION BY CRP.
RC   STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX   PubMed=10856643; DOI=10.1111/j.1574-6968.2000.tb09146.x;
RA   Hutchings M.I., Drabble W.T.;
RT   "Regulation of the divergent guaBA and xseA promoters of Escherichia coli
RT   by the cyclic AMP receptor protein.";
RL   FEMS Microbiol. Lett. 187:115-122(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8548458; DOI=10.1038/nsb0196-74;
RA   Tesmer J.J.G., Klem T.J., Deras M.L., Davisson V.J., Smith J.L.;
RT   "The crystal structure of GMP synthetase reveals a novel catalytic triad
RT   and is a structural paradigm for two enzyme families.";
RL   Nat. Struct. Biol. 3:74-86(1996).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC         Evidence={ECO:0000269|PubMed:9890911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11681;
CC         Evidence={ECO:0000305|PubMed:9890911};
CC   -!- ACTIVITY REGULATION: Inhibited by 2-fluoroinosine 5'-monophosphate (F-
CC       IMP) and by N(2)-hydroxyguanosine 5'-monophosphate (N(2)-OH-GMP).
CC       {ECO:0000269|PubMed:9890911}.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       P04079; P04079: guaA; NbExp=3; IntAct=EBI-909122, EBI-909122;
CC   -!- INDUCTION: Activated by cAMP receptor protein (CRP). Repressed by DnaA.
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DR   EMBL; M10101; AAB18619.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75560.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16394.1; -; Genomic_DNA.
DR   PIR; A24640; SYECGU.
DR   RefSeq; NP_417002.1; NC_000913.3.
DR   RefSeq; WP_000138270.1; NZ_LN832404.1.
DR   PDB; 1GPM; X-ray; 2.20 A; A/B/C/D=1-525.
DR   PDBsum; 1GPM; -.
DR   AlphaFoldDB; P04079; -.
DR   SMR; P04079; -.
DR   BioGRID; 4259645; 51.
DR   DIP; DIP-9852N; -.
DR   IntAct; P04079; 8.
DR   STRING; 511145.b2507; -.
DR   DrugBank; DB04272; Citric acid.
DR   MEROPS; C26.957; -.
DR   jPOST; P04079; -.
DR   PaxDb; 511145-b2507; -.
DR   EnsemblBacteria; AAC75560; AAC75560; b2507.
DR   GeneID; 947334; -.
DR   KEGG; ecj:JW2491; -.
DR   KEGG; eco:b2507; -.
DR   PATRIC; fig|1411691.4.peg.4230; -.
DR   EchoBASE; EB0415; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_6; -.
DR   InParanoid; P04079; -.
DR   OMA; IWQSFAV; -.
DR   OrthoDB; 9802219at2; -.
DR   PhylomeDB; P04079; -.
DR   BioCyc; EcoCyc:GMP-SYN-MONOMER; -.
DR   BioCyc; MetaCyc:GMP-SYN-MONOMER; -.
DR   BRENDA; 6.3.5.2; 2026.
DR   UniPathway; UPA00189; UER00296.
DR   EvolutionaryTrace; P04079; -.
DR   PRO; PR:P04079; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IDA:EcoCyc.
DR   GO; GO:0003921; F:GMP synthase activity; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IMP:EcoCyc.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.30.300.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00344; GMP_synthase; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_GATase.
DR   InterPro; IPR022955; GMP_synthase.
DR   InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00884; guaA_Cterm; 1.
DR   NCBIfam; TIGR00888; guaA_Nterm; 1.
DR   PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR   PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Direct protein sequencing;
KW   Glutamine amidotransferase; GMP biosynthesis; Ligase; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome.
FT   CHAIN           1..525
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140123"
FT   DOMAIN          9..207
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          208..400
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT   ACT_SITE        181
FT   ACT_SITE        183
FT   BINDING         235..241
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   CONFLICT        3
FT                   /note="E -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..14
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           20..29
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           43..49
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           87..95
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          107..115
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   TURN            120..124
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   TURN            171..174
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          175..180
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           190..199
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           210..225
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          229..233
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           238..251
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          255..261
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           269..277
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   TURN            278..281
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          285..289
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           291..298
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           304..325
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          326..333
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           338..343
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   TURN            375..378
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           381..390
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           418..437
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           441..443
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          444..457
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   TURN            460..462
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          465..479
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          482..485
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   HELIX           490..503
FT                   /evidence="ECO:0007829|PDB:1GPM"
FT   STRAND          507..513
FT                   /evidence="ECO:0007829|PDB:1GPM"
SQ   SEQUENCE   525 AA;  58679 MW;  D934786DFF3D694B CRC64;
     MTENIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIRDFN PSGIILSGGP
     ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EASNEREFGY AQVEVVNDSA
     LVRGIEDALT ADGKPLLDVW MSHGDKVTAI PSDFITVAST ESCPFAIMAN EEKRFYGVQF
     HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS
     SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVLDMFGDH FGLNIVHVPA EDRFLSALAG
     ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN
     VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY
     CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF
     MTAHWAHLPY DFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE
//