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Database: UniProt
Entry: H7GHJ0_9DEIN
LinkDB: H7GHJ0_9DEIN
Original site: H7GHJ0_9DEIN 
ID   H7GHJ0_9DEIN            Unreviewed;       503 AA.
AC   H7GHJ0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
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:EIA38720.1};
GN   ORFNames=RLTM_08679 {ECO:0000313|EMBL:EIA38720.1};
OS   Thermus parvatiensis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=456163 {ECO:0000313|EMBL:EIA38720.1, ECO:0000313|Proteomes:UP000053186};
RN   [1] {ECO:0000313|EMBL:EIA38720.1, ECO:0000313|Proteomes:UP000053186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL {ECO:0000313|EMBL:EIA38720.1,
RC   ECO:0000313|Proteomes:UP000053186};
RX   PubMed=22689228; DOI=10.1128/JB.00604-12;
RA   Dwivedi V., Sangwan N., Nigam A., Garg N., Niharika N., Khurana P.,
RA   Khurana J.P., Lal R.;
RT   "Draft genome sequence of Thermus sp. strain RL, isolated from a hot water
RT   spring located atop the Himalayan ranges at Manikaran, India.";
RL   J. Bacteriol. 194:3534-3534(2012).
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:EIA38720.1}.
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DR   EMBL; AIJQ01000015; EIA38720.1; -; Genomic_DNA.
DR   RefSeq; WP_008633169.1; NZ_AIJQ01000015.1.
DR   PATRIC; fig|456163.3.peg.1697; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000053186; 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   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}.
FT   DOMAIN          190..378
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51553"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00344,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         217..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ   SEQUENCE   503 AA;  56064 MW;  14FF68C8963EDAD1 CRC64;
     MVLVLDFGSQ YTRLIARRLR ELRVFSLILP GRASLEEILK HKPQALILSG GPNSVFDPDA
     PRPDPRLFSL GLPILGICYG MQLLAQELGG RVERSGRAEY GKALLTRHEG XLFRGXEGEV
     QVWMSHQDAV TELPPGWRVV AETEENPVAA MEAPDGKTFA VQFHPEVAHT PKGMQILENF
     LEIAGVKRDW TPEHVLESLV KEVRERVGED RVLLAVSGGV DSSTLALLLA KARVNHLAVF
     VDHGLLRLGE REEVEGALKA LGVNLRVVDA RERFLKALKG VEDPEEKRRI IGREFVEVFS
     LVAREAGPFR FLAQGTLYPD VIESAGEPGA AKIKSHHNVG GIPEDLKFEL LEPFRLLFKD
     EVRELALLLG LPDPIRLRHP FPGPGLAVRI LGEVTEEKLD ILRRADDIFI SLLREWGLYS
     QVAQALAVLT PVRSVGVAGD ERKYGYVLAL RAVTTEDFMT ADWARLPLDF LDEAARRITR
     RVPEIGRVVY DLTSKPPATI EWE
//
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