ID   GUAA_LACLM              Reviewed;         513 AA.
AC   Q9Z6H4; A2RJZ5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=llmg_1008;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10048028; DOI=10.1046/j.1365-2958.1999.01222.x;
RA   Duwat P., Ehrlich S.D., Gruss A.;
RT   "Effects of metabolic flux on stress response pathways in Lactococcus
RT   lactis.";
RL   Mol. Microbiol. 31:845-858(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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; AF058326; AAD15805.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97602.1; -; Genomic_DNA.
DR   RefSeq; WP_011834939.1; NZ_WJVF01000022.1.
DR   AlphaFoldDB; Q9Z6H4; -.
DR   SMR; Q9Z6H4; -.
DR   STRING; 416870.llmg_1008; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; CAL97602; CAL97602; llmg_1008.
DR   GeneID; 61109720; -.
DR   KEGG; llm:llmg_1008; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; KRKIIGH; -.
DR   PhylomeDB; Q9Z6H4; -.
DR   BioCyc; LLAC416870:LLMG_RS05125-MON; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000364; Chromosome.
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..513
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140137"
FT   DOMAIN          8..198
FT                   /note="Glutamine amidotransferase type-1"
FT   DOMAIN          199..388
FT                   /note="GMPS ATP-PPase"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   BINDING         226..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        298
FT                   /note="K -> Q (in Ref. 1; AAD15805)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  56888 MW;  3DEC53AEBD4BC483 CRC64;
     MSDTTLEKII VLDYGSQYNQ LIARRIREIG VFSELMSHKV TAKEIREINP IGIILSGGPN
     SVYDEGSFDI DPEIFELGLP VLGICYGMQL MSYKLGGMVE AAGEREYGVA PLQLTEKSAL
     FAGTPEVQDV LMSHGDRVTA IPEGFHVVGT SPNSPFAAVE NTERNLYGIQ FHPEVRHSVH
     GTEMLRNFAL NICGAKGNWS MENFIDMQIK DIREKVGDKK VLLGLSGGVD SSVVGVLLQR
     AIGDQLTSIF VDHGFLRKGE ADQVMETLGG KFGLNIIKVD AQKRFMDKLV GLSDPETKRK
     IIGNEFVYVF DDEANKLEGV DFLAQGTLYT DVIESGTDTA QTIKSHHNVG GLPEDMQFQL
     IEPLNTLFKD EVRALGTQLG MPDEIVWRQP FPGPGLAIRV LGDLTEEKLE TVRESDAILR
     EEIAASGLER DVWQYFTVNT DVKSVGVMGD QRTYDYTLAI RAITSIDGMT ADFAQLPWDL
     LQKISKRIVN EVDHVNRIVY DITSKPPATV EWQ