ID A0A1F6AQ63_9BACT Unreviewed; 553 AA.
AC A0A1F6AQ63;
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=A2960_01505 {ECO:0000313|EMBL:OGG26825.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_39_12b.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798388 {ECO:0000313|EMBL:OGG26825.1, ECO:0000313|Proteomes:UP000176609};
RN [1] {ECO:0000313|EMBL:OGG26825.1, ECO:0000313|Proteomes:UP000176609}
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:OGG26825.1}.
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DR EMBL; MFJR01000007; OGG26825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6AQ63; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000176609; 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..267
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 308..547
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 553 AA; 62606 MW; AB22928B38CF6DDC CRC64;
MPLKYIFVSG GVISGLGKGI SSGSIAFLLQ SAGFRVTLVK CENYLNIDAG TINPIEHGDP
FLCEDGTEAD MDIGTYEKFL DKNMHRHNFV TMGQVYKTVI DRERRFEYNG EDVEAIPHIT
NEITDRINKA AETDRAQIVI VELGGTVGEY QNLFYYEAAR ILTLKRPKDV IHVHVSYLPT
PSHLGEPKTK PTQQSVRALN SAGIQPDFIV ARSEKPLDKR RRDRFSLFCN MRPEDIISSP
DAETVYEVPL QFHAQGLLQK ICQKLSLSYK DPDLGKWELL IGKIKAKKDR KITIAIVGKY
FATGEYQLRD SYAALMDAID HASWALGVKV NTNWIDAEKV EKEGIEKYVD QNINGLIVPI
GWGERGAEGM IKAAGWARNN KVPYLGLCYG MQLAVISFAR DILGWRDANT TENDKKTTHP
VIHLMPAQKQ FMERRSYGGT MRLGAWKAIV KKDTIAWGSY EKYNQFIDKS KGLTSERHRH
RYEFNDAYAK NFDNKGLIIA ARSVVENLVE IVELPKSVHP FYLGTQGHPE YKSRPLSPHP
IFLEFLEACI NKK
//
