ID A0A1G2F8R3_9BACT Unreviewed; 541 AA.
AC A0A1G2F8R3;
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=A2Y98_03965 {ECO:0000313|EMBL:OGZ34454.1};
OS Candidatus Portnoybacteria bacterium RBG_19FT_COMBO_36_7.
OC Bacteria; Candidatus Portnoybacteria.
OX NCBI_TaxID=1801992 {ECO:0000313|EMBL:OGZ34454.1, ECO:0000313|Proteomes:UP000179099};
RN [1] {ECO:0000313|EMBL:OGZ34454.1, ECO:0000313|Proteomes:UP000179099}
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:OGZ34454.1}.
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DR EMBL; MHMW01000009; OGZ34454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2F8R3; -.
DR STRING; 1801992.A2Y98_03965; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000179099; 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 3..266
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 306..535
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 541 AA; 60874 MW; 3123B95385EBDD64 CRC64;
MAKYIFVVGG VMSGVGKGVA TASIGKIIQA RGFSVTAIKI DPYVNVDAGT MNPTEHGEVF
VLDEGMECDQ DMGNYERFLD MNLPAINYMT TGSIYEAVIH RERNMGYEGK CVEVVPHIPL
EVIDRIEKAI KKAKADFITI EIGGTAGEYQ NVLFLEAARM LKLKKPHDVL FVLVSYLPIP
SKIGEMKTKP TQYAVRALNS VGIQPDIILA RSSVPLDKKR KEKIALNCNI HEQDVISAPD
IQTIYEVPIN FEKDKLSDLI LEKLEIKAKK SDMKEWNALV KTIRAKKSGL KIGIVGKYFG
TGDFILSDAY ISVIEAIKHA AFFHKKEPHV EWINSEAFEK DPKSIKSLKN YDGIIVPGGF
GFRGIEGKIK AIEYCRKNKI PYLGLCYGMQ LMVIEFARHV CGLRDAHTTE IDRETKYPVI
DIMPEQKKVL EDKNYGATMR LGAYPAALEM RTQAFAAYKK HLVSERHRHR WEVNPEYIEI
LEKNGLIFSG KSPDGRLMEI AELPAKLHPF FVGTQFHPEF KSKPLAPHPL FREFIGAAIK
I
//
