ID   A0A0G0KTE9_9BACT        Unreviewed;       770 AA.
AC   A0A0G0KTE9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=ribonucleoside-triphosphate reductase (thioredoxin) {ECO:0000256|ARBA:ARBA00012275};
DE            EC=1.17.4.2 {ECO:0000256|ARBA:ARBA00012275};
GN   ORFNames=UT05_C0005G0013 {ECO:0000313|EMBL:KKQ82037.1};
OS   Parcubacteria group bacterium GW2011_GWF2_38_76.
OC   Bacteria.
OX   NCBI_TaxID=1618960 {ECO:0000313|EMBL:KKQ82037.1, ECO:0000313|Proteomes:UP000034258};
RN   [1] {ECO:0000313|EMBL:KKQ82037.1, ECO:0000313|Proteomes:UP000034258}
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:KKQ82037.1}.
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DR   EMBL; LBVI01000005; KKQ82037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0KTE9; -.
DR   STRING; 1618960.UT05_C0005G0013; -.
DR   Proteomes; UP000034258; 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; -; 2.
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          17..112
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   770 AA;  87681 MW;  8FFE42D7556264FC CRC64;
     MPEEKKINKK KPTKMPTKMV KRDGTVVEFD INRITNAVSK AMEVAKEGKE EDARFVAHSV
     VKELATMIAD DRSYIPTVED TQDIIENELI MMSYPKTAKA FIIYREKRAE LRRQTGAVVH
     EEVRRLVNES KKYFRNPLSE FVFYSSYSKW IPEKGRRETW LETVGRYVDF MKENLGKKMS
     EEEYEEVRSY MLSMKTLGSM RLLWAAGKAT RSTNVAAYNC AFVAPKCWQD FGEIMYVLMC
     GTGIGFSVER QNVEMLPIIK RQTGKKLPKH FVEDSKEGWA NAFVLGLNTW AEGGDVEFDY
     SKVRPQGARL ATMGGRASGP EPLKALLDFS RSKIMSRQGR HLTTLDVHDI VCKTGEVVVM
     GGVRRSALIS LSELDDPEMR DAKSGQFYLA HPERSMANNS VVYNEKPTVV QFLEEWISLM
     KSGSGERGIF NRGSLFKQMP ERRWKLFEKD SYDSGINPCG EIILRSKQFC NLSEIVARKE
     DTEKTLIEKA RIAAILGTYQ ATLTKFPYLS KEWKRNCEEE ALLGVSITGQ WDCKAVRDPK
     TLEKMKTMVI ETNKKYAKKF GINPATAATC VKPSGNGSQL FDSSSGCHPR HSKYYLRRVR
     VENHNPLFMM LKDMGVPYSP EVGQDENNAK TYVLEFPIKS PDGAIVKNDL SAIDQLEYWK
     ILKLNFTEHN PSVTISVSNG EWLKVGSAVY DNWDIVGGLS FLPRDEHVYR LAPYETITEE
     EYKKRAAVFP EIDFSKLVLY EYDDQTKGSK ELACTAGLCE IEPLPDGNKK
//