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GUAA_BRUC2
ID   GUAA_BRUC2              Reviewed;         520 AA.
AC   A9MEB0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344};
DE            EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344};
DE   AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; OrderedLocusNames=BCAN_B0364;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00344}.
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:0000255|HAMAP-Rule:MF_00344};
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}.
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DR   EMBL; CP000873; ABX63548.1; -; Genomic_DNA.
DR   RefSeq; WP_004690106.1; NC_010104.1.
DR   AlphaFoldDB; A9MEB0; -.
DR   SMR; A9MEB0; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; ABX63548; ABX63548; BCAN_B0364.
DR   GeneID; 45053415; -.
DR   GeneID; 55592054; -.
DR   KEGG; bcs:BCAN_B0364; -.
DR   HOGENOM; CLU_014340_0_5_5; -.
DR   OMA; KRKIIGH; -.
DR   PhylomeDB; A9MEB0; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000001385; Chromosome II.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..520
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120226"
FT   DOMAIN          9..202
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          203..395
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         230..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   520 AA;  57069 MW;  1EC07D39D0731EC2 CRC64;
     MSTTAYPDTI LIIDFGSQVT QLIARRVREA NVYCEIVPFQ SADEAFKRLQ PKGVILSGSP
     HSTTDIGSPR APQAIFDAGI PVLGICYGEQ TMCAQLGGNV ESGHDREFGR AFLDVQEDSP
     LFAGIWAKGT RHQVWMSHGD RVTSLPDGFT IIGTSPNAPY AVIADEKRKY YGVQFHPEVV
     HTPDGAKLLQ NFVHRIVGVK PGWTMGAYRE QAVEAIRKQV GSGKVICALS GGVDSSVAAL
     LAHEAVGDQL TCILVDHGLM RKDEAQQVVE MFREHYNLPL ILVDASDRFI GALEGESDPE
     KKRKTIGRLF IEVFEEEARK LGGADFLVQG TLYPDVIESV SFTGGPSVTI KSHHNVGGLP
     ERMKMQLVEP LRELFKDEVR LLGKELGLPD SFIGRHPFPG PGLAIRCPGG VTRGKLEILR
     EADAIYLDEI RKAGLYDAIW QAFAVLLPVQ TVGVMGDGRT YEFVCALRAV TSVDGMTADF
     YHYDMNFLGN AATRIINEVR GINRVVYDVT SKPPGTIEWE
 
 
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