NRDJ_STRAW
ID NRDJ_STRAW Reviewed; 964 AA.
AC Q82KE2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SAV_2461;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(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; BA000030; BAC70172.1; -; Genomic_DNA.
DR RefSeq; WP_010983898.1; NZ_JZJK01000086.1.
DR AlphaFoldDB; Q82KE2; -.
DR SMR; Q82KE2; -.
DR STRING; 227882.SAV_2461; -.
DR EnsemblBacteria; BAC70172; BAC70172; SAVERM_2461.
DR KEGG; sma:SAVERM_2461; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_11; -.
DR OMA; WACADPG; -.
DR OrthoDB; 357568at2; -.
DR Proteomes; UP000000428; Chromosome.
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 Pfam; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
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..964
FT /note="Vitamin B12-dependent ribonucleotide reductase"
FT /id="PRO_0000231661"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 365
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 363..367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 553..557
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 159..376
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 964 AA; 105012 MW; 2C634475A49C6B42 CRC64;
MTETASGPAR GSRAKGTKAK GLRIERIHTT PGVHPYDEVE WARRDVVMTN WRDGSVNFEQ
RGVEFPDFWS VNAVNIVTSK YFRGAVGTPQ REVSLRQLID RIVKTYRKAG EDYKYFASPA
DAEIFEHELA YALLHQIFSF NSPVWFNVGT PQPQQVSACF ILAVDDSMES ILDWYKEEGM
IFKGGSGAGL NLSRIRSSKE LLSSGGNASG PVSFMRGADA SAGTIKSGGA TRRAAKMVIL
DVDHPDIEDF IETKVKEEEK IRALRDAGFD MDLGGDDITS VQYQNANNSV RVNDTFMKAV
EEGGKFGLTS RMTGEVIEEV DAKSLFRKMA EAAWACADPG IQYDDTINHW HTCPESGRIN
GSNPCSEYMH LDNTSCNLAS LNLMKFLKDD GKGRQSFEVE RFAKVVELVI TAMDISICFA
DFPTQKIGEN TRAFRQLGIG YANLGALLMA TGHAYDSDGG RALAGAITSL MTGTSYKRSA
ELAAVVGPYD GYARNAQPHQ RVMKQHSDAN GVAVRVDDLD TPIWAAATEA WQDVLHLGEK
NGFRNAQASV IAPTGTIGLA MSCDTTGLEP DLALVKFKKL VGGGSMQIVN GTVPQALRRL
GYQEEQIEAI VAHIAENGNV IDAPGLKHEH YEVFDCAMGE RSISAMGHVR MMAAIQPWIS
GALSKTVNLP ETATVEDVEE VYFEAWKMGV KALAIYRDNC KVGQPLSAKK KETEKAEVTA
KTEATIREAV EKVVEYRPVR KRLPKGRPGI TTSFTVGGAE GYMTANSYPD DGLGEVFLKM
SKQGSTLAGM MDAFSIAVSV GLQYGVPLET YVSKFTNMRF EPAGMTDDPD VRMAQSIVDY
IFRRLALDFL PFETRSALGI HSAEERQRHL ETGSYEPSDD VDMDVEGLAQ SAPRAQELKA
VATPKAEVAA AVPAPKQAHT SAELVEMQLG IQADAPLCFS CGTKMQRAGS CYICEGCGST
SGCS
