ID A0A1G2QIP8_9BACT Unreviewed; 551 AA.
AC A0A1G2QIP8;
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=A2589_03330 {ECO:0000313|EMBL:OHA59841.1};
OS Candidatus Vogelbacteria bacterium RIFOXYD1_FULL_46_19.
OC Bacteria; Candidatus Vogelbacteria.
OX NCBI_TaxID=1802439 {ECO:0000313|EMBL:OHA59841.1, ECO:0000313|Proteomes:UP000177838};
RN [1] {ECO:0000313|EMBL:OHA59841.1, ECO:0000313|Proteomes:UP000177838}
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:OHA59841.1}.
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DR EMBL; MHTK01000005; OHA59841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QIP8; -.
DR STRING; 1802439.A2589_03330; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000177838; 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 7..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 311..541
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 522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 524
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 551 AA; 61598 MW; A145FAB5828291AB CRC64;
MKKNKTKYIF VVGGVMSGVG KGITSSSLAA IMQARGFRTT AIKIDPYINV DAGTMNPTEH
GEVFVLGDGD ECDQDMGNYE RFLDTDLSRT NYMTTGRVYL EVIRRERNLE YEGKNVEVVP
DIPKEVIRRI ERAGREASAD VVVVEIGGTI GEYQNIIFLE AGRMMKTKYP DDVAFVMVSY
LPIPSKVGEM KTKPTQYASR SLNSVGVQAD VIIARSEMAL DKKRKDKIAT FCNIVPERVI
SAPDIDSIYE VPINFERDRL GEIMCQILKL GNHRTTELTA WKKLVRQIKT VKRPLNIAIV
GKYFDSGEFV LSDVYISVIE ALKLSAYQAG VKPVLSYVNS KDIETGKRRV TELAKYDGII
VPGGFGTAGI EGLVKVIKFA REKKIPYFGL CYGMQLLVIE YARHKAGVPG ATSREIDPTA
SDLVIDVMEE QKKNLADKNY GGTMRLGSFP AYLKKGTLAR GAYKAEMVTE RHRHRYEVNP
AYIERLEKAG LVFSGTSPSG QLMEIAELPK TDHPFFLGTQ FHPEFLARPL RPHPLFSEFV
KAAKDHHPKT K
//
