ID A0A1F6M3T6_9BACT Unreviewed; 547 AA.
AC A0A1F6M3T6;
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=A3B90_02215 {ECO:0000313|EMBL:OGH66249.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_41_13.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798676 {ECO:0000313|EMBL:OGH66249.1, ECO:0000313|Proteomes:UP000178742};
RN [1] {ECO:0000313|EMBL:OGH66249.1, ECO:0000313|Proteomes:UP000178742}
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:OGH66249.1}.
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DR EMBL; MFPX01000022; OGH66249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6M3T6; -.
DR STRING; 1798676.A3B90_02215; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000178742; 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..272
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 312..540
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 392
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 547 AA; 61279 MW; 85465A7585158C6B CRC64;
MPKKTKNRKY VFVIGGVMSS VGKGVTSASI SKILQARGYK TTNVKCDMYV NLDAGTIRPI
EHGEVFVGED GIEADQDLGN YERFTGNTMT ALNYLTTGQV YNEVIRRERN LEYEGEDVEV
VPDIPNEIIR RIKQAAQKND AEVTVVEFGG TVGEYQLLLF LEAARMMKFS NPDDIAIVLV
SYLPIPPHIG EMKTKPTQYA SRSLNEAGLQ ADFIVARGSA ELDKRRRERL ATFCNVLKDN
AISAPNVETI YEVPMSLEKG ELGNKLLKKL GLKSRRNTIA EWEKFVHHIK SLKKEVHIAV
VGKYFGTGSY TLSDSYISVI ESIKHASWAN NVKPVLSWVN SEDFEKDPAS VKDLAKFDGI
IVPGGFGERG VDGILAAIQF AREKKVPYLG LCYGLQLACV EFARNVLGYK DANTTEVNPK
TGNPIIYANP MQAKNIQEKK YGATMRLGSY DCLLKKGTKV YKAYGEELIS ERHRHRYEFN
NKYLEEMDNA GLRAVGINPE TELLEMIELD NHPFFVGTQA HPEFKSRPQE PHPLFREFVK
AAVKGGK
//
