ID A0A1L8QWJ5_9ENTE Unreviewed; 515 AA.
AC A0A1L8QWJ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=GMP synthetase {ECO:0000256|HAMAP-Rule:MF_00344};
DE AltName: Full=Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00344};
GN Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN ORFNames=RU93_GL001122 {ECO:0000313|EMBL:OJG11889.1};
OS Enterococcus aquimarinus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG11889.1, ECO:0000313|Proteomes:UP000182149};
RN [1] {ECO:0000313|EMBL:OJG11889.1, ECO:0000313|Proteomes:UP000182149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG11889.1,
RC ECO:0000313|Proteomes:UP000182149};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC {ECO:0000256|ARBA:ARBA00002332, ECO:0000256|HAMAP-Rule:MF_00344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP +
CC diphosphate + 2 H(+); 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:0000256|HAMAP-Rule:MF_00344};
CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00005153, ECO:0000256|HAMAP-
CC Rule:MF_00344}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00344}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJG11889.1}.
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DR EMBL; JXKD01000002; OJG11889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8QWJ5; -.
DR STRING; 328396.RU93_GL001122; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000182149; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 1.
DR FunFam; 3.30.300.10:FF:000002; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.620:FF:000001; GMP synthase [glutamine-hydrolyzing]; 1.
DR FunFam; 3.40.50.880:FF:000001; GMP synthase [glutamine-hydrolyzing]; 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 NCBIfam; NF000848; PRK00074.1; 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 PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00344};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00344};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00344};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00344}; Reference proteome {ECO:0000313|Proteomes:UP000182149}.
FT DOMAIN 198..390
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT ACT_SITE 171
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT ACT_SITE 173
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344"
FT BINDING 225..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 515 AA; 57146 MW; 557AC6B596A8971F CRC64;
MPNVEKIIVL DYGSQFNQLI TRRIREFGVF SELLSHRITA DEVKAINPKG IILSGGPNSV
YADNAFDIDE EILNLGIPVL GICYGMQLIT HKLGGKVEGA DKKEYGKAEL NIKLDEAPLF
GATPKNQVVW MSHGDLVTEV PAGFEVVATS NDCPIAAMQN RDRQIYGVQF HPEVRHTEYG
TDLLKQFAFD ICGAAGDWSM ENFIEIEIAK IRQQVGDKKV LLGLSGGVDS SVVGVLLQKA
IGDQLTCIFV DHGLLRKNEG DQVMEMLGNK FGLNIIRVDA KDRFLDKLAG VRDPEQKRKI
IGNEFVYLFD DEAKKIAGSK KVSFLAQGTL YTDVIESGTE TAQTIKSHHN VGGLPDDMDF
ELIEPLNTLF KDEVRALGTE LGMPDDIVWR QPFPGPGLGV RVLGEITEEK LEIVRESDAI
LREEIKIAGL DRDIWQYFTV LPGIRSVGVM GDGRTYDYTI GIRAITSIDG MTADFARIPW
DVLQKISVRI VNEVAHVNRI VYDITSKPPA TVEWE
//
