NRDJ_LEPIN
ID NRDJ_LEPIN Reviewed; 1201 AA.
AC Q8F3P1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=LA_2360;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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}.
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DR EMBL; AE010300; AAN49559.2; -; Genomic_DNA.
DR RefSeq; NP_712541.2; NC_004342.2.
DR RefSeq; WP_000783498.1; NC_004342.2.
DR AlphaFoldDB; Q8F3P1; -.
DR SMR; Q8F3P1; -.
DR STRING; 189518.LA_2360; -.
DR EnsemblBacteria; AAN49559; AAN49559; LA_2360.
DR KEGG; lil:LA_2360; -.
DR PATRIC; fig|189518.3.peg.2342; -.
DR HOGENOM; CLU_000404_0_1_12; -.
DR InParanoid; Q8F3P1; -.
DR Proteomes; UP000001408; 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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..1201
FT /note="Vitamin B12-dependent ribonucleotide reductase"
FT /id="PRO_0000231660"
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; 133948 MW; E62F8C198030B8A6 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 DFTLVKFKKL 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