ID A0A1F5I2B1_9BACT Unreviewed; 541 AA.
AC A0A1F5I2B1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=A3A60_03160 {ECO:0000313|EMBL:OGE10516.1};
OS Candidatus Curtissbacteria bacterium RIFCSPLOWO2_01_FULL_42_26.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797729 {ECO:0000313|EMBL:OGE10516.1, ECO:0000313|Proteomes:UP000179227};
RN [1] {ECO:0000313|EMBL:OGE10516.1, ECO:0000313|Proteomes:UP000179227}
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:OGE10516.1}.
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DR EMBL; MFBS01000010; OGE10516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5I2B1; -.
DR STRING; 1797729.A3A60_03160; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000179227; 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; 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 4..266
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 307..533
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 514
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 516
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 541 AA; 60557 MW; 7E8A13B34AB642AE CRC64;
MTTKVIFVSG GVISGIGKGV ATSSIALLLK SRGFRVTTIK ADPYLNVDAG TLNPIEHGEV
FVLDDGMECD QDLGNYERFL NQNLNATNYM TTGQIFKTVI EKERALGFEG KTVEFFQDPP
REIIKRIYNC AKVNNAEIVL FEIGGTVGEY QNLLFLEANR LLKLNHPRDI LHVHLTYLPI
PSSIGEMKSK PAQMSILQLA QSGIHADVVL ARSQVAVDDK RKEKIAISCG LNPEDIISAP
DVESIYQVPL NFENQELSGQ ILKKLNTRPR KSDLADWKVM VNRILTAKKT ARIAMVGKYF
STGDFTLTDA YLSVIESIRH AAAHFDFKPK LRWVDSEQIE KSGAGILKGF DGIIVPGGFG
ARAVEGIVEA VKFARENNVP YFGLCYGMQQ AAIDFARNVL GYKDANTTEI NPNTQHPVID
VMENQKEKIK NRNLGGTMRL GSWDFKAKKG TIVAKAYGKI EGSERHRHRY EFNDKYKKEF
EKNGMIVSAT SKEGNLVEAM EIQDHPFFVG VQFHPELKSR PLHPHPLYMA FMEAVSKQKR
K
//
