ID A0A0S1S894_9FLAO Unreviewed; 510 AA.
AC A0A0S1S894;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ECO:0000313|EMBL:ALM06663.1};
GN ORFNames=SB49_01715 {ECO:0000313|EMBL:ALM06663.1};
OS Sediminicola sp. YIK13.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM06663.1, ECO:0000313|Proteomes:UP000063759};
RN [1] {ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA Kwon Y.M., Kim S.-J.;
RT "Genome sequence of Sediminicola sp. YIK13.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM06663.1, ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|EMBL:ALM06663.1,
RC ECO:0000313|Proteomes:UP000063759};
RX PubMed=26823585;
RA Kwon Y.M., Kim S.J.;
RT "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT Bacterium Sediminicola sp. YIK13.";
RL Genome Announc. 4:e01635-15(2016).
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}.
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DR EMBL; CP010535; ALM06663.1; -; Genomic_DNA.
DR RefSeq; WP_062053263.1; NZ_CP010535.1.
DR AlphaFoldDB; A0A0S1S894; -.
DR STRING; 1453352.SB49_01715; -.
DR KEGG; syi:SB49_01715; -.
DR PATRIC; fig|1453352.4.peg.357; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000063759; Chromosome.
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; 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 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; 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:UP000063759}.
FT DOMAIN 194..385
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 167
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 BINDING 221..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 510 AA; 56592 MW; C86EB0B8DF4ADC56 CRC64;
MQNNVLILDF GSQYTQLIAR RVRELNIFCE IKPYNHLPED LSEYKAVILS GSPFSVRAED
APHPDLSQIR GKKPLLGVCY GAQYLAHFNG GSVEGSNTRE YGRAKLSYVK ENEPFFDKIS
KGSQVWMSHA DTIKELPENT TRLASTHDVE NAAYKFNGEE SYAIQFHPEV YHTTDGKQLL
ENFLVHIAGV AQTWTPDAFV ETTVTELKSK IGQDKVILGL SGGVDSTVAA ILLHKAIGKH
LHCIFVNNGL LRKNEFEDVL HQYKDMGLNV KGVDASARFL DALAGESDPE KKRKAIGRVF
IEVFDDESHL VEDAKWLAQG TIYPDVIESV SATGGPSATI KSHHNVGGLP DFMKLNVVEP
LRMLFKDEVR RVGASMGIDK ALLGRHPFPG PGLAIRILGD ITPEKVAILQ EVDAIFINGL
KEWGLYDKVW QAGAMLLPVN SVGVMGDERT YEKCVALRAV ESTDGMTADW VNLPYEFLQK
TSNDIINKVR GVNRVVYDIS SKPPATIEWE
//
