ID A0A1F6W5V8_9BACT Unreviewed; 534 AA.
AC A0A1F6W5V8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, 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=A3D42_01660 {ECO:0000313|EMBL:OGI77224.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_02_FULL_41_18.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801754 {ECO:0000313|EMBL:OGI77224.1, ECO:0000313|Proteomes:UP000177777};
RN [1] {ECO:0000313|EMBL:OGI77224.1, ECO:0000313|Proteomes:UP000177777}
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:OGI77224.1}.
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DR EMBL; MFUE01000017; OGI77224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6W5V8; -.
DR STRING; 1801754.A3D42_01660; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000177777; 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 1..255
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 294..523
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 534 AA; 59657 MW; 828C93E31E3FBDA0 CRC64;
MSSVGKGIAA ASIGKILQSR GYHVANLKAD MYVNLDAGTI RPAEHGEVFV GEDGIEADQD
LGNYERFTDQ VSVREDYITT GQIYAEVIKR ERNLEYGGED VEVYPDIPKE IIRRIEVCQK
KNKSEITIIE YGGTVGEGQL LTFLEATRMM KASNPSDVLL VLISYLPTPS LLGEQKSKPT
QRAITDLHSV GLNPDFVICR SDKPATTDIK RTISNVCSLP IERIISAPDV YSIYDVPVNF
EKENFGTTLL TTLGLPPRSK DLADWTKLAE KIKKIKKNVH IGIVGKYFNF KSCKDTYISV
IESINHAAWA LGYKPDIVWL DSEIYEGDKR KLKELDNLDG IVVPGGFGKR GTEGMILTAD
YARRRKIPYF GLCLGMQIMT ISWARNVLGH KNANSVELDA DTPYPVIATM SDQVEKIKNK
NYGASMRLGA YPAHLQKGSV AESAYGVSKI SERHRHRYEV NPEYISALEK SGLVFSGRSP
DGILMEIAEL PKREHPFYLG TQFHPEFKSR PLSPHPLFAA FLKACVSRKR KVFL
//
