ID A0A1E2RWC0_9HYPH Unreviewed; 515 AA.
AC A0A1E2RWC0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 18-JUN-2025, entry version 36.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000256|ARBA:ARBA00021562, ECO:0000256|HAMAP-Rule:MF_00344};
DE EC=6.3.5.2 {ECO:0000256|ARBA:ARBA00012746, 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=A7A08_02647 {ECO:0000313|EMBL:ODA66524.1};
OS Methyloligella halotolerans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Hyphomicrobiaceae; Methyloligella.
OX NCBI_TaxID=1177755 {ECO:0000313|EMBL:ODA66524.1, ECO:0000313|Proteomes:UP000095087};
RN [1] {ECO:0000313|EMBL:ODA66524.1, ECO:0000313|Proteomes:UP000095087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM B-2706 {ECO:0000313|EMBL:ODA66524.1,
RC ECO:0000313|Proteomes:UP000095087};
RA Vasilenko O.V., Doronina N.V., Poroshina M.N., Tarlachkov S.V.,
RA Trotsenko Y.A.;
RT "Draft genome sequence of Methyloligella halotolerans C2T (VKM B-2706T=CCUG
RT 61687T=DSM 25045T), a halotolerant polyhydroxybutyrate accumulating
RT methylotroph.";
RL Submitted (JUL-2016) 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:ODA66524.1}.
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DR EMBL; MASI01000007; ODA66524.1; -; Genomic_DNA.
DR RefSeq; WP_069095811.1; NZ_MASI01000007.1.
DR AlphaFoldDB; A0A1E2RWC0; -.
DR STRING; 1177755.A7A08_02647; -.
DR PATRIC; fig|1177755.3.peg.2670; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000095087; 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; 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:UP000095087}.
FT DOMAIN 198..390
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 81
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; 56368 MW; 7CBF4D237C8F5D31 CRC64;
MTERVLIVDF GSQVTQLIAR RVREAGVYSE IVPFDKAEAD LKEKSAAAII LSGGPASVAE
SDTPRAPQAV FEAGLPVLGI CYGEQAMVAQ LGGTVEPHNS KEFGRADLEV VESTPLFDGV
WPKGETHPVW MSHGDRVTKL PDGFKTIAVS HGAPFAAIAN EERKMYGVQF HPEVVHTPRG
AEIIGNFVRN IAGLEGDWTM AHFKDVEIAK IRDQVGGGKV ICGLSGGVDS SVAAILIHEA
IGDQLACIFV DHGLLRQDER AQVENLFRET YNIPLVVVDA SERFLAALKD IDDPEQKRKI
IGKLFIDVFD EEAKKLGEVD FLAQGTLYPD VIESVSFSGG PSVTIKSHHN VGGLPERMRM
KLVEPLRELF KDEVRALGRE LGLPDAFVDR HPFPGPGLAI RIPGAVSEDK LAILRQADAI
YLDEIRAAGL YDTIWQAFAV LLPVRTVGVM GDARTYDYVC ALRAVTSTDG MTADYYDFSH
DFLGRAARRI INEVRGINRV VYDITSKPPG TIEWE
//
