ID A0A1F6PAK6_9BACT Unreviewed; 543 AA.
AC A0A1F6PAK6;
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=A2563_01185 {ECO:0000313|EMBL:OGH93202.1};
OS Candidatus Magasanikbacteria bacterium RIFOXYD1_FULL_40_23.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798705 {ECO:0000313|EMBL:OGH93202.1, ECO:0000313|Proteomes:UP000176634};
RN [1] {ECO:0000313|EMBL:OGH93202.1, ECO:0000313|Proteomes:UP000176634}
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:OGH93202.1}.
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DR EMBL; MFRA01000001; OGH93202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6PAK6; -.
DR STRING; 1798705.A2563_01185; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000176634; 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 6..270
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 310..537
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 390
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 543 AA; 60925 MW; 86F9717EEDAF3CF8 CRC64;
MSSKTKYIFV IGGVLSGVGK GVTTASIGRI FKNRGFNVSA IKIDPYINVD AGTMNPVEHG
EVFVTEDGDE TDQDLGNYER FLETDIYSFN YMTTGRVYLS VIEKERSMYY KGKCVEVVPH
IPMEVIGRIK TAAAKTKAEV MVIEVGGTAG EYQNILFLEA ARMMKLENPE SVAFVLVSYL
PVPGHLGEMK TKPTQYASRT LNASGIQADF IVARGPAALD KPRREKLAVL CGLRSEDDVI
AAPDVKSIYE IPQVLEKQKF AELLMKRLKI KPRKLTDKGW DSFVNKIDKI EKSIKIAVVG
KYFATGDYTL SDSYISVINA IKHAAWHNGV NAELTWVDAE EYEKNPGKVK ELGKYDALIV
PGGFGTRGIE GIISAIKYAR ENNLPYLGLC YGMQLATIEF SRNVLGYKDA HTVECNPKSK
NLIINVNLTQ ADNIKNERYG GTMRLGAYDC DLKPGSHARE QYKTDKISER HRHRYEFDNK
YREEMESKGM EVTGVNPQSN LVEIVELKKH PYFVGVQFHP EFKSRFLQPH PLFVGLVRAV
LKK
//
