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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//