ID A0A1F6G180_9BACT Unreviewed; 556 AA.
AC A0A1F6G180;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=A3H16_01910 {ECO:0000313|EMBL:OGG91879.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_12_FULL_53_8.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798529 {ECO:0000313|EMBL:OGG91879.1, ECO:0000313|Proteomes:UP000178601};
RN [1] {ECO:0000313|EMBL:OGG91879.1, ECO:0000313|Proteomes:UP000178601}
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:OGG91879.1}.
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DR EMBL; MFMQ01000030; OGG91879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6G180; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000178601; 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 9..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 313..548
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 556 AA; 61156 MW; B85F629E0D629433 CRC64;
MKRARAGHKY IFVVGGVMSG VGKGTATASI GKLLTARGLS VNLVKIDPYL NVDAGTMNPT
EHGEVFVLDS GLETDQDMGN YERFLGRDLG PEDYMTSGMV YKAVIERERN LGYGGKCVEA
IPHVRDEIVE RLERSARMAK SDVTVVEIGG TLGDFSNALF IDAARVMPLK HPSDVLFVMV
SYLPVPNTIG EMKTKPTQNA VRQLNAYGVQ PDVILARSTH TLDKKRKEKL AIWCNVQADH
IISAPDVDSI YDVPLNFERD KLSEVLMSLL GKRAKQGADF SQWREFAEHA HNGNGVVKIG
IVGKYFDTGD FVLSDAYFSV IEAIKFSAYA HGVRPEIAWL NAKAYEIDPT SVSELKGYDG
IIVPGGFGET GVEGKINAIR FARENTIPYF GLCYGMQLMT IEYARNVAGL SGAHTTEIEA
STPHPVIAIL PEQIEKLAKK NYGGSMRLGA YPCELMEGSI ASESYKLQAT SHKLISERHR
HRFEVNPEYI GKLESAGLVF SGKSPDGRLM EIAELPKSVH PFMLGTQFHP ELRARPLSPH
PLFNAFIKAA IGKKHP
//
