ID A0A1F5KA14_9BACT Unreviewed; 535 AA.
AC A0A1F5KA14;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=A3F00_04340 {ECO:0000313|EMBL:OGE37654.1};
OS Candidatus Daviesbacteria bacterium RIFCSPHIGHO2_12_FULL_37_11.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1797777 {ECO:0000313|EMBL:OGE37654.1, ECO:0000313|Proteomes:UP000176527};
RN [1] {ECO:0000313|EMBL:OGE37654.1, ECO:0000313|Proteomes:UP000176527}
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:OGE37654.1}.
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DR EMBL; MFDE01000038; OGE37654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5KA14; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000176527; 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 2..265
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 305..530
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 382
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 511
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 535 AA; 59943 MW; 80F9B47C0473588F CRC64;
MKYIFVSGGV ISGIGKGIAT SSIALLLKSA GYKVSPLKID PYLNIDAGTM NPIHHGEVFV
LDDGSETDQD LGNYERFLNE DLNKANYTTS GQVYLSVIQR ERALEYDGEC VEAVPHIPEE
INKRIENAGK SMNADIVVIE IGGTVGELQN VFIFEANRLL KQKKSDDVLH VHVSYLPVPA
SIGEMKSKPV QMSVRELNSM GIQPDILLAR SEVKIDDTRR KKLGLFCNIS AEDIIAAPDV
KSIYEVPVNF EEENLTERIL GKLKLKRKNK DLREWRKFTN KIKSAEKQIK IGIVGKYFST
GDFTLSDSYV SVIEAIKHAS WTQGFNPEIT WVDSGKILSD LSLLSNLDGV IVPGGFGSRD
IDGKIEAIKY CRENKISYLG LCYGMQMAVI EYARNVLRLQ NANTTEIDPG TKFPVIHIMP
DQEKKMLERD YGASMRLGAW DCKLKPGTMA KKLYGKSEIS ERHRHRYEFN NQYLKELVKN
GMVISGTSPD GKLVEIIELK GHPFFVGTQF HPELKSRPLN PHPLFMGFIK AASLH
//
