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Database: UniProt
Entry: G6XGP0_9PROT
LinkDB: G6XGP0_9PROT
Original site: G6XGP0_9PROT 
ID   G6XGP0_9PROT            Unreviewed;       531 AA.
AC   G6XGP0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
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|ARBA:ARBA00031356, ECO:0000256|HAMAP-Rule:MF_00344};
GN   Name=guaA {ECO:0000256|HAMAP-Rule:MF_00344};
GN   ORFNames=GMO_06550 {ECO:0000313|EMBL:EHH69348.1};
OS   Gluconobacter morbifer G707.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH69348.1, ECO:0000313|Proteomes:UP000004949};
RN   [1] {ECO:0000313|EMBL:EHH69348.1, ECO:0000313|Proteomes:UP000004949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G707 {ECO:0000313|EMBL:EHH69348.1,
RC   ECO:0000313|Proteomes:UP000004949};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT   gut.";
RL   Submitted (OCT-2011) 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:EHH69348.1}.
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DR   EMBL; AGQV01000001; EHH69348.1; -; Genomic_DNA.
DR   RefSeq; WP_008850805.1; NZ_AGQV01000001.1.
DR   AlphaFoldDB; G6XGP0; -.
DR   STRING; 1088869.GMO_06550; -.
DR   PATRIC; fig|1088869.3.peg.663; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   OrthoDB; 9802219at2; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000004949; 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; 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; 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:UP000004949}.
FT   DOMAIN          214..406
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         241..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   531 AA;  58630 MW;  166F3EFDAC34AFDE CRC64;
     MTQQDVSTVE KLDETLHEDR ILILDFGSQV TQLIARRVRE SGVYCEIWPF TASEEKIRDF
     NPRGIILSGS PASVHDENAP PVPGVVFALN RPVLGICYGQ QAMCQMLGGK VETHEHREFG
     RAYIDIAEDC SLFRGVWARG KREQVWMSHG DRVTQLPPGF RAVAHSEGAP FAIIADEGRR
     LYGVQFHPEV VHTPHGAALI RNFTHNVAGC SGTWTMAGFR DLEIARIRKQ VGSGRVICGL
     SGGVDSSVAA KLIHDAIGDQ LTCIFVDPGI LRSGEADEVV KTFRGRFNIR LVHRDASELF
     LRELAGVTDP EVKRKTIGRL FIEVFEEEAA KLGGAQFLAQ GTLYPDVIES VSFSGGPSVT
     IKSHHNVGGL PERMNMQLVE PLRELFKDEV RALGRELGIP ENIVGRHPFP GPGLAIRIPG
     DVTKEKLDLL RKVDAIYLEE IRNAGLYDAI WQAFAVLLPV RTVGVMGDGR TYDQACALRA
     VTSTDGMTAE VYPFDFAFLN RVAGRIVNEV RGINRVTYDI TSKPPGTIEW E
//
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