ID   A0A0G0AU89_9BACT        Unreviewed;       789 AA.
AC   A0A0G0AU89;
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=UR19_C0003G0006 {ECO:0000313|EMBL:KKP30170.1};
OS   Candidatus Nomurabacteria bacterium GW2011_GWF1_31_48.
OC   Bacteria; Candidatus Nomurabacteria.
OX   NCBI_TaxID=1618767 {ECO:0000313|EMBL:KKP30170.1, ECO:0000313|Proteomes:UP000034934};
RN   [1] {ECO:0000313|EMBL:KKP30170.1, ECO:0000313|Proteomes:UP000034934}
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:KKP30170.1}.
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DR   EMBL; LBOG01000003; KKP30170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0AU89; -.
DR   PATRIC; fig|1618767.3.peg.245; -.
DR   Proteomes; UP000034934; 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   Gene3D; 3.90.1390.10; b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3; 1.
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          16..113
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   789 AA;  90090 MW;  E2541A2BD2746690 CRC64;
     MEKDFILGKE ELIKIKNIRN REGEIIPFNI NKIADAVYKA FLITNEGEKK EAKDVATKVF
     HKLVNLKIKS KEKKFIPTVE IIQDLVEAEL MDLGYHSTAK SYILYRSKRA ELRREVGTVP
     PENKKVFDES SSYFVSSYEE FIFYRTYSKW QDGLGRRETW VETIDRFMIY MKENLGNKLS
     SRDYSDVREG ILNQEICPSM RLLWSAGEAC KKTNVWAYNC SYIAPSAWQD LGETMYILMC
     GAGLGFSIES ETVQKFPQIR RQTGKKLATH FVEDSKEGWA DAYVLGCKTW ADGYDIDFDY
     SKVRPSGARL KIAGGRASGP QPLIDLMNFT KKKILARQAK RLTNLDLHDI ICQIGLIVVA
     GGVRRSALIS LSDIDDESMR KSKQGQFWID NGQRSMANNS AVYNQKPSAS EFLNEWLELI
     KSGTGERGIF NRGGLMTQLP KRRIENWKEA GIIDDQNVIV GLPGSNPCGE ITLRSKQFCN
     LTSIVVRPKD SIEDLKRKVR LSTILGTYQA TLTHFGYLSK EWKNNCDDEA LLGVSITGYY
     DNQIIRSDDV LSKLREESIK TNREYAKKFG IKYSTCITTI KPHGNSGQLL YVGSGMHPWY
     AEYYIRRVRI STNDPLFQLI KDQGVPFKAE VGYSTSNSTV AVVEFPIKAP EGAITRDKVS
     AIDLLNEWKR LKVNYIEHNP SVTIYVGEDE WIKVANFVYE NWDIVGGLSF LPRSEHVYQL
     APYEEISKEE YNRRIKEIKH IDFSKLIYYE QEDNTVGAKE FACVSGVCSV DDVLAEEAQK
     EKMEDPLDK
//