ID A0A1F6C308_9BACT Unreviewed; 564 AA.
AC A0A1F6C308;
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=A2841_02390 {ECO:0000313|EMBL:OGG43422.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_48_10.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798476 {ECO:0000313|EMBL:OGG43422.1, ECO:0000313|Proteomes:UP000178249};
RN [1] {ECO:0000313|EMBL:OGG43422.1, ECO:0000313|Proteomes:UP000178249}
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:OGG43422.1}.
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DR EMBL; MFKP01000041; OGG43422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6C308; -.
DR UniPathway; UPA00159; UER00277.
DR Proteomes; UP000178249; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..284
FT /note="CTP synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06418"
FT DOMAIN 325..555
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 564 AA; 62164 MW; 6C9827598451C517 CRC64;
MVVTRSSQRR SGSAPSKKRH KYIFVIGGVM SGVGKGIATS SIGLILQSKG YKVNAVKIDP
YLNVDAGTMN PTEHGEVFVL SSGLETDQDM GNYERFLNTS LAPEDYMTSG MVYQHVLNRE
RNLGYGGRCV EAIPHVRDEI IRRIRLATDQ NGSDISVIEI GGTVGDFQNA LFIEAARVMK
LEHPDDVVFV LVSYLPIPGN LGEMKTRPTQ NAVHQLNSYG VQASFVVARS AQPLDQKRKE
KIAISCNVTP EHIISAPDVD SIYDVPLNFE KEHIGDMLLK TLHLPKKAAK GLREWGHFVS
KVRTAKKELS IAIVGKYFDT GDFVLSDAYL SVIEAIKYSA AEVGAKAKIT WVNAKDFEKN
ASSVSLLADF DGILVPGGFG ETGIEGKIRA IQYAREHKIP YFGLCYGMQL LLVEYARNVL
GLAGSHTTEI DSDTTHPVID VMPEQKDIIA KADYGGTMRL GTYPAKLKKG TIAREAYGTD
EIEERHRHRY EVNPAYVKNF EEGGIVFSGV SPSGVLMEIA ELPKDVHPFM MGTQFHPELQ
ARPLAPHPLF TAFLKACVAQ HARR
//
