ID   GUAA_LACLA              Reviewed;         513 AA.
AC   Q9CFJ0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=LL1486; ORFNames=L115968;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05584.1; -; Genomic_DNA.
DR   PIR; F86810; F86810.
DR   RefSeq; NP_267642.1; NC_002662.1.
DR   RefSeq; WP_003130105.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFJ0; -.
DR   SMR; Q9CFJ0; -.
DR   STRING; 272623.L115968; -.
DR   MEROPS; C26.957; -.
DR   PaxDb; Q9CFJ0; -.
DR   EnsemblBacteria; AAK05584; AAK05584; L115968.
DR   KEGG; lla:L115968; -.
DR   PATRIC; fig|272623.7.peg.1596; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000002196; 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; Reference proteome.
FT   CHAIN           1..513
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_0000140136"
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"
SQ   SEQUENCE   513 AA;  56781 MW;  20D64580E00C5C19 CRC64;
     MSDTTLEKII VLDYGSQYNQ LIARRIREIG VFSELMSHKV TAKEIREINP IGIILSGGPN
     SVYDEGSFDI DPEIFELGLP VLGICYGMQL LSYKLGGMVE AAGEREYGVA PLQLTGKSAL
     FAGTPEVQDV LMSHGDRVTA IPEGFHVVGT SPNSPFAAVE NTERNLYGIQ FHPEVRHSVH
     GTEMLRNFAL NICGAKGNWS MENFIDMQIK NIREKVGDKK VLLGLSGGVD SSVVGVLLQR
     AIGDQLTSIF VDHGFLRKGE ADQVMETLGG KFGLNIIKVD AQKRFMDKLV GLSDPETKRK
     IIGNEFVYVF DDEANKLEGV DFLAQGTLYT DVIESGTDTA QTIKSHHNVG GLPEDMQFQL
     IEPLNTLFKD EVRALGTQLG MPDEIVWRQP FPGPGLAIRV LGDLTEEKLE TVRESDAILR
     EEIAAAGLER DVWQYFTVNT DVKSVGVMGD QRTYDYTLAI RAITSIDGMT ADFAQLPWDL
     LQKISKRIVN EVDHVNRIVY DITSKPPATV EWQ