ID A0A0G1VX07_9BACT Unreviewed; 552 AA.
AC A0A0G1VX07;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0000256|ARBA:ARBA00012291};
DE EC=6.3.4.2 {ECO:0000256|ARBA:ARBA00012291};
GN ORFNames=UY49_C0010G0007 {ECO:0000313|EMBL:KKW11011.1};
OS Microgenomates group bacterium GW2011_GWC1_49_7.
OC Bacteria.
OX NCBI_TaxID=1618530 {ECO:0000313|EMBL:KKW11011.1, ECO:0000313|Proteomes:UP000034729};
RN [1] {ECO:0000313|EMBL:KKW11011.1, ECO:0000313|Proteomes:UP000034729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW11011.1}.
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DR EMBL; LCQE01000010; KKW11011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VX07; -.
DR PATRIC; fig|1618530.3.peg.146; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000034729; 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 313..550
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 391
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 552 AA; 61827 MW; 0833F1A35540881E CRC64;
MPTKFIFVSG GVISGLGKGI TTASIALLLQ NRGYNVTPVK CENYLNMDAG LINPIEHGDP
FLCDDGTEAD MDMGTYEKFL GKNMYRHNFV TMGQIYQSVI ERERNFGYEG EDVEAIPHVT
DEIIKRIKAA GEKENADVVV IELGGTAGEY QNALYYEASR ILSRKKGNTV IHVHVSYLPT
PSHLGEPKTK PTQLSVRTLN SMGIQPDFIV TRAEKAMDAR RRARFALFCN VEPENVIDSV
DLPSAYETPL YLAKQKLDEK ILTMMNLPLR KLDIGDWERM VGSIEKSRRA GSRSGGKTIA
IVGKYFATGE YQLRDSYAAL MDAIDHAAWA QGVDVQVKWI QAEKLEKGDI TELKDVDGII
VPIGWGPRGV EGKIAAVHYA RVNKIPYLGL CYGMQLAVVE YGRNVLGLEG ANTLEVDSDT
RHPVIHMIKG QDEILRRRAY GGTMRLGRWE CKVKPGTITD TAYSKHKGYD DVDKKIVGER
HRHRYEFNDA YAQKFEDAGL VIAGRSVVEN LAEIIELPKS VHPFFLGTQY HPEYRSRPLA
PHPIFLEYIK AL
//
