ID   NRDJ_LEPIC              Reviewed;        1201 AA.
AC   Q72S00;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleoside-diphosphate reductase NrdJ;
GN   Name=nrdJ; OrderedLocusNames=LIC_11587;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC       deoxyribonucleotides. May function to provide a pool of
CC       deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC       and/or for immediate growth after restoration of oxygen (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250};
CC       Note=5'-deoxyadenosylcobalamine (coenzyme B12). {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS70183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016823; AAS70183.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000783496.1; NC_005823.1.
DR   AlphaFoldDB; Q72S00; -.
DR   SMR; Q72S00; -.
DR   PaxDb; Q72S00; -.
DR   EnsemblBacteria; AAS70183; AAS70183; LIC_11587.
DR   GeneID; 61144885; -.
DR   KEGG; lic:LIC_11587; -.
DR   HOGENOM; CLU_000404_0_1_12; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd02888; RNR_II_dimer; 1.
DR   InterPro; IPR013678; RNR_2_N.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR   InterPro; IPR029072; YebC-like.
DR   Pfam; PF08471; Ribonuc_red_2_N; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 2.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF75625; SSF75625; 1.
DR   TIGRFAMs; TIGR02504; NrdJ_Z; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Disulfide bond; DNA synthesis; Nucleotide-binding;
KW   Oxidoreductase.
FT   CHAIN           1..1201
FT                   /note="Vitamin B12-dependent ribonucleotide reductase"
FT                   /id="PRO_0000231659"
FT   REGION          1100..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        482
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        484
FT                   /note="Cysteine radical intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        486
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         482..486
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         683..687
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        199..495
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1201 AA;  133918 MW;  062F88B39A9A120C CRC64;
     MKMNRHFTVP QNGESSTIQW TKRNSKITNP DGSKVFEAND ILVPEDWSQV AVDILAQKYF
     RRKGVPKYLK KVQEDGIPEW LQKSIPDTEK LESLKPEDRF GGETSALEVF HRLAGCWTYW
     GYKYKYFSDE ESAKIFYDEI VYMLATQMAA PNSPQWFNTG LNWAYGIDGK SQGHYYVDPS
     TGKLVKSTSA YEHPQPHACF IQSVDDDLVN EGGIMDLWVR EARLFKYGSG TGTNFSNLRG
     ENEPLSGGGK SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VCLDVDHPDI ENFIDWKVTE
     EKKVASLVTG SMLNNRHLNA IMSACYEMEG EDRFNPKKNS SLKKTIQDAK KVLIPDNYIK
     RVIDLARQGY KEILFEELTT DWQSDAYNTV SGQNSNNSIR LTNEFMAAVE QDQPWNLYFR
     TEKEKAKVEG RKAKPSQTLR ARELWEKISY AAWASADPGT QYHTTINEWH TCPEDGPINA
     SNPCSEYMFL DNTACNLASA NLQKFVNLET LNFDVEGFRY LCKLWTIILE ISVTMAQFPS
     KEIAELSYKF RTLGLGYANL GSVLMVLGIP YDSQQAMAIT GAISSIMHMT AYATSAEMAK
     EQGPFVGYAK NQKHMLRVIR NHRRAAYNAP SGDYEGLTIT PIGINPAFCP SYMLKAAQED
     ADLALSLGEK YGFRNAQVTV IAPTGTIGLV MDCDTTGIEP DFALVKFKKL AGGGYFKIIN
     QSVPYGLKKL GYSPSEIEAI VNYCKGHATL NGAPVINTQA LKEKGFTNEI LEKVEASLPL
     AFDINFAFNK FNLGENFLTK NLGISKEIFD SPGFSLLEHL GFTKEDINKA NDYVCGTMTI
     ENAPFLKEKD YPVFDCANKC GKYGKRFLSY ESHIRIMAAA QPFISGAISK TINLPEEAVI
     EDIKNAYFLS WKMMIKANAL YRDGSKLSQP LNSVLELLNG IEIDDQEEIR EATISKDPVQ
     IAEKIVTKYI SHRRKLPSRR AGYTQKAIVG GHKVYLRTGE YEDGQIGEIF IDMHKEGAAF
     RSLMNAFAIS VSLGLQHGVP LEEYVDAFTF FKFEPNGIVS GNKHIKMSTS VIDYIFRELA
     ITYLGRYDLG QVAPEDLRGD EIGSKRATAE SNGQEKETLS SMTAVIEPTP KKEVETISYS
     QMISKEKPSS SPSGISLLEE VKLAKIKGYT GDSCSECGSF EMVRNGSCLK CMSCGSTTGC
     S