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Database: UniProt
Entry: A0A1G2KRX7_9BACT
LinkDB: A0A1G2KRX7_9BACT
Original site: A0A1G2KRX7_9BACT 
ID   A0A1G2KRX7_9BACT        Unreviewed;       556 AA.
AC   A0A1G2KRX7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE            EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN   ORFNames=A3C16_00740 {ECO:0000313|EMBL:OHA02198.1};
OS   Candidatus Sungbacteria bacterium RIFCSPHIGHO2_02_FULL_51_29.
OC   Bacteria; Candidatus Sungbacteria.
OX   NCBI_TaxID=1802273 {ECO:0000313|EMBL:OHA02198.1, ECO:0000313|Proteomes:UP000177811};
RN   [1] {ECO:0000313|EMBL:OHA02198.1, ECO:0000313|Proteomes:UP000177811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC         glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000314};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007533}.
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:OHA02198.1}.
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DR   EMBL; MHQL01000042; OHA02198.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2KRX7; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000177811; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03113; CTPS_N; 1.
DR   CDD; cd01746; GATase1_CTP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR033828; GATase1_CTP_Synthase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00337; PyrG; 1.
DR   PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR   PANTHER; PTHR11550:SF0; CTP SYNTHASE-RELATED; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          3..264
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          310..538
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        390
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   556 AA;  62389 MW;  04BF05177DB6AA19 CRC64;
     MARFIFVCGG VMSGIGKGVS TASIARLLKE RGFRVTACKI DPYLNVDAGT MNPTEHGEVF
     VTEDGVECDQ DIGNYERFLG QDIPRENYMT TGLIYQTVIE RERNLEYEGK CVEVIPHIPE
     EVIRRLDRAG KKAKADFVLV EIGGTVGEYQ NALFLEAGRI LRLQRPGDVL FVLVSYLPVP
     KLVGEMKTKP TQYAVRSMNT AGLQPDIIIA RSVVPLDEPR KKKISIFCNI APEDVISAPD
     IKSIYEIPLN FERDHLSERL LLKFGIKAKK RSLGEWDVFV KKMRRANKPE TPAVRIGIVG
     KYFGTGNFVL SDSYISVIEA VKHATWHFGK RPEIEWLNAE EYEGNPSSLK LLKRFDGIIV
     PGGFGSRGVE GKIAVIRFCR VSNIPFFGLC YGMQLATVEF ARHACRLRDA HTTEVKGAAA
     HPVIHTLPEQ LVNIKERRLG GSMRLGAYTC ALKPGTKSYK AHGSALISER HRHRYEFNGD
     FRDQLETCGL IVSGVNTERN LVEIIELRGH PFFVGTQFHP EFKSRPLAPH PLFIEFIRAG
     IKKSRMHAPE KAGARR
//
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