ID   A0A0G1TJ25_9BACT        Unreviewed;       765 AA.
AC   A0A0G1TJ25;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE            EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN   ORFNames=UY07_C0009G0016 {ECO:0000313|EMBL:KKU81779.1};
OS   Parcubacteria group bacterium GW2011_GWA1_47_8.
OC   Bacteria.
OX   NCBI_TaxID=1618793 {ECO:0000313|EMBL:KKU81779.1, ECO:0000313|Proteomes:UP000034272};
RN   [1] {ECO:0000313|EMBL:KKU81779.1, ECO:0000313|Proteomes:UP000034272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001283};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC       reductase family. {ECO:0000256|ARBA:ARBA00005654}.
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:KKU81779.1}.
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DR   EMBL; LCOP01000009; KKU81779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TJ25; -.
DR   STRING; 1618793.UY07_C0009G0016; -.
DR   PATRIC; fig|1618793.3.peg.325; -.
DR   Proteomes; UP000034272; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.70.20; -; 3.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          21..116
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   765 AA;  87077 MW;  B9DDB1F1825C969F CRC64;
     MQKNTKQAKT SAVVPHKSPI VSVRKRSGSI VPFDIEHIVS AVNKAMRSTG EGDRKEAEYI
     ARKVESELKR ISKLVKDFIP TVEGMQDIAE KELILEEYVK TAKAYILYRE ERARAREKQG
     EIPEEVKKMV AEGKKYFRSP MSEFVYYRSY SRWLPEQGRR ETWIETVDRY VAFMKENLGS
     KMTEKEYAEI RQAILEQQVM PSMRLLWSAG DAARKTNVTG YNCSFIAPSC VQDLAEIMYL
     LMCGTGVGYS VESQNAQMFP QIKKQTGKML PTHTVVDSKE GWADAYALGM NTWFSGGDIK
     FDYSKLRPAG ARLMTMGGKS SGPEPLISLI DFSRERVMKK QGRRLSNLDL HDIICKIGEV
     VVSGGVRRSA LISLSDLDDH DMRHAKDGQF YLTDPQRMMA NNSAVYWQKP SNAEFLDEWV
     SLMKAGSGER GIFNRGSIPK QMPARRWKTL EKDFDTCGTN PCGEIILKSK QFCNLSEIVA
     RAEDTEASLM KKARLASILG TYQSSLTNFG YLSKEWKENC EEERLLGVSI TGQWDCKTVR
     NPEVMRKLRD EAVKVNKEYA KRFGINPSSA VTAVKPSGTV SQLVDASSGM HPRNSEYYIR
     RIRIAATDSL FKMMKDQGVT YHPEVGQSVE SAVTYVLEFP VRAPEKSIYK NDQSALEQLE
     YWKMVKENFT EHNPSVTISV GEEEWISVAN WLYENWEMIG GLSFLPRSNH VYRLAPYEEI
     TKEKYEEMVK KFPDIDFSKI VSYEREDHTQ GSKELACVAG ICEIA
//