ID   GUAA_VIBCH              Reviewed;         517 AA.
AC   Q9KTW2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA; OrderedLocusNames=VC_0768;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; AE003852; AAF93933.1; -; Genomic_DNA.
DR   PIR; D82282; D82282.
DR   RefSeq; NP_230417.1; NC_002505.1.
DR   RefSeq; WP_000164597.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KTW2; -.
DR   SMR; Q9KTW2; -.
DR   STRING; 243277.VC_0768; -.
DR   MEROPS; C26.957; -.
DR   DNASU; 2615311; -.
DR   EnsemblBacteria; AAF93933; AAF93933; VC_0768.
DR   GeneID; 57739478; -.
DR   GeneID; 66941509; -.
DR   KEGG; vch:VC_0768; -.
DR   PATRIC; fig|243277.26.peg.732; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_6; -.
DR   OMA; KRKIIGH; -.
DR   BioCyc; VCHO:VC0768-MON; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01742; GATase1_GMP_Synthase; 1.
DR   CDD; cd01997; GMP_synthase_C; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   Gene3D; 3.40.50.880; -; 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   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00884; guaA_Cterm; 1.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..517
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140203"
FT   DOMAIN          9..199
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          200..392
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   BINDING         227..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  57764 MW;  80AC2194E1172CA5 CRC64;
     MTKNIHDQRI LILDFGSQYT QLVARRVREI GVYCELWSWD VEEADIREFN PDGIILSGGP
     ESVTEANSPR APQYVFDSGV PVFGVCYGMQ TMAEQLGGRV ATSDEREFGY AQVKISGESA
     LFKDLDLTQD VWMSHGDKVV EIPADFVKIG ETDTCPYAAM ANEEKKYYGV QFHPEVTHTK
     NGLQMLENFV LGVCGCERLW TSESIIEDAV ARIKEQVGND EVILGLSGGV DSSVVAMLVH
     RAIGSKLTCV FVDNGLLRLN EGEQVMEMFG DKFGLNIIKV DAEERFLKAL EGIDEPEAKR
     KTIGRVFVEV FDEESKKLSN AKWLAQGTIY PDVIESAASK TGKAHVIKSH HNVGGLPDDM
     KMGLVEPLRE LFKDEVRKIG LELGLPYNML YRHPFPGPGL GVRVLGEVKK EYCDLLRRAD
     AIFIEELHAA DLYNKVSQAF TVFLPVRSVG VMGDGRKYDW VVSLRAVETI DFMTAHWAHL
     PYEFLGKVSN RIINEVNGIS RVVYDISGKP PATIEWE