ID A0A255I9A6_9FIRM Unreviewed; 513 AA.
AC A0A255I9A6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=C8E03_103278 {ECO:0000313|EMBL:PXV91717.1}, CG710_012830
GN {ECO:0000313|EMBL:RDY30780.1};
OS Lachnotalea glycerini.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnotalea.
OX NCBI_TaxID=1763509 {ECO:0000313|EMBL:RDY30780.1, ECO:0000313|Proteomes:UP000216411};
RN [1] {ECO:0000313|EMBL:RDY30780.1, ECO:0000313|Proteomes:UP000216411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY30780.1,
RC ECO:0000313|Proteomes:UP000216411};
RX PubMed=29051240;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Raymond F.,
RA Brodeur S., Corbeil J., Isabel S., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of a Sporulating and Motile Strain of Lachnotalea
RT glycerini Isolated from Water in Quebec City, Canada.";
RL Genome Announc. 5:e01059-17(2017).
RN [2] {ECO:0000313|EMBL:PXV91717.1, ECO:0000313|Proteomes:UP000247523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28816 {ECO:0000313|EMBL:PXV91717.1,
RC ECO:0000313|Proteomes:UP000247523};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDY30780.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCRI-19302 {ECO:0000313|EMBL:RDY30780.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) 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=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: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:RDY30780.1}.
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DR EMBL; QICS01000003; PXV91717.1; -; Genomic_DNA.
DR EMBL; NOKA02000028; RDY30780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255I9A6; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000216411; Unassembled WGS sequence.
DR Proteomes; UP000247523; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd01997; GMP_synthase_C; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00884; guaA_Cterm; 1.
DR NCBIfam; TIGR00888; guaA_Nterm; 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; PF03054; tRNA_Me_trans; 1.
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 SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 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:UP000216411}.
FT DOMAIN 196..388
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 223..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 513 AA; 56752 MW; E660297B91741C27 CRC64;
MEREMVLVLD FGGQYNQLIA RRVRECNVYC EIHSYNISLE KIKEMNPKGI IFTGGPNSVY
GEDSPRCGKE IFELGIPILG ICYGSQLMSY VLGGSVKTAP VSEYGKTEVL VNKNSLMFGD
VSEKTICWMS HTDYIEKAPE GFQVTASTPV CPVAAMESPE KKLYATQFHP EVMHTQEGTK
MLRNFLFKLC ECSGDWKMDS FVDHAIEAIR KKVGDGKVLC ALSGGVDSSV AAVMLAKAVG
KQLTCVFVDH GLLRKNEGDE VEAVFGPEGP YDLNFIRVNA QDRFFAKLAG VEEPEAKRKI
IGEEFIRVFE DEAKKIGTVD FLVQGTIYPD VIESGLGKSA VIKSHHNVGG LPDYVDFKEI
IEPLRDLFKD EVRKAGLELG IPEYLVYRQP FPGPGLGIRI IGDVTPEKVH MVQEADAIYR
EEIAKAGVDK GLGQYFAALT NMRSVGVMGD ERTYDYAIAL RAVTTSDFMT AEAAELPWEV
LGKVTSRIVN EVKGVNRVLY DCTGKPPATI EFE
//
