ID A0A1B1YV67_9GAMM Unreviewed; 524 AA.
AC A0A1B1YV67;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ECO:0000313|EMBL:ANX04533.1};
GN ORFNames=PG2T_10335 {ECO:0000313|EMBL:ANX04533.1};
OS Immundisolibacter cernigliae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Immundisolibacterales;
OC Immundisolibacteraceae; Immundisolibacter.
OX NCBI_TaxID=1810504 {ECO:0000313|EMBL:ANX04533.1, ECO:0000313|Proteomes:UP000092952};
RN [1] {ECO:0000313|Proteomes:UP000092952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR3.2 {ECO:0000313|Proteomes:UP000092952};
RA Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT "Complete genome sequence of Solimmundus cernigliae, representing a novel
RT lineage of polycyclic aromatic hydrocarbon degraders within the
RT Gammaproteobacteria.";
RL Submitted (MAR-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=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; CP014671; ANX04533.1; -; Genomic_DNA.
DR RefSeq; WP_068804924.1; NZ_CP014671.1.
DR AlphaFoldDB; A0A1B1YV67; -.
DR STRING; 1810504.PG2T_10335; -.
DR KEGG; gbi:PG2T_10335; -.
DR InParanoid; A0A1B1YV67; -.
DR OrthoDB; 9802219at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000092952; 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; 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 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:UP000092952}.
FT DOMAIN 207..399
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 234..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 524 AA; 57101 MW; 145ED1D163EB1C3E CRC64;
MTDLHADRIL ILDFGSQYTQ LIARRVRELG VYSEIHPWDM DAAALRAFAP KGIILSGGPE
SVTEAGSPRA PEVVWSLGVP VLGICYGMQT MAVQLGGAVE PGAVKEFGYA EIRAHGHSRL
LDGIEDRVNA EGHGLLDVWM SHGDRVSALP EGFKRIASTA DVPLAGMADE ARGYYAFQFH
PEVTHTTQGT RIYARFVHEI CGCGNAWTPG NIIEDAIAAV RRQVGDGKVL LGLSGGVDSS
VVAALLHKAI GDQLTCVFVD NGLLRHQEGD QVMQVFARNL GVKVIRVDAE ARFLDALRGV
ADPEAKRKII GGLFIDVFDE QAARIEGVDF LAQGTIYPDV IESAGSKTGK AHVIKSHHNV
GGLPEHMKLK LVEPLRELFK DEVRAIGLEL GLPAEMVQRH PFPGPGLGVR ILGEVTKAAA
DTLRLADHIF IEELRRAGWY ERTSQAFAVY LPVKSVGVTG DGRRYEPVVA LRAVETVDFM
TARWAHLPYE LLDLCSRRII NEVPGLSRVV YDVSGKPPAT IEWE
//