ID B0R617_HALS3 Unreviewed; 1051 AA.
AC B0R617;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdJ {ECO:0000313|EMBL:CAP14186.1};
GN Synonyms=nrdA2 {ECO:0000313|EMBL:CAP14186.1};
GN OrderedLocusNames=OE_3328R {ECO:0000313|EMBL:CAP14186.1};
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=478009 {ECO:0000313|EMBL:CAP14186.1, ECO:0000313|Proteomes:UP000001321};
RN [1] {ECO:0000313|EMBL:CAP14186.1, ECO:0000313|Proteomes:UP000001321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1 {ECO:0000313|Proteomes:UP000001321};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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.
CC {ECO:0000256|RuleBase:RU364064}.
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 Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR EMBL; AM774415; CAP14186.1; -; Genomic_DNA.
DR RefSeq; WP_010903197.1; NC_010364.1.
DR AlphaFoldDB; B0R617; -.
DR EnsemblBacteria; CAP14186; CAP14186; OE_3328R.
DR GeneID; 68694313; -.
DR KEGG; hsl:OE_3328R; -.
DR HOGENOM; CLU_000404_2_1_2; -.
DR PhylomeDB; B0R617; -.
DR Proteomes; UP000001321; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin 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 Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 28..170
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 174..769
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 980..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 115312 MW; 40B5F50D49C8F76A CRC64;
MSSEDLSADD LTLPVKRVTG DSLEDRLTAN AYHNILPARY LRKDTDGEHV ESQEDLFERV
AKNIALAEVV FESDDPVTAT PSQLKPDHPR RDELAAEVFG SDVDPDSETA TVELTDSNIN
KFAYDTVVPE LDDPEVREHV EGVAAEFQDL MASLSFMPNS PTLMNAGDEL QQLSACFVDS
PDDDITDIHQ TAKEAAEVFQ SGGGMGYAFW QLRPYGDTVG STGGIASGPL TFMETFDQMC
ETIAQGGARR GAQMAVMRVS HPDVVEFIHA KNKDVSLAQT LKLNDPDDYT YTEFSEALEE
ARDLIDEDGR VPEHLRNAVE GHLSNFNISV GVTDGFMEAL EAGEEYTFTN PRTGEAHIAT
EETKEMYSRY GLGHYVTPGE ELTLPAEELW SRIVEGAHEN GEPGVIYLER VNDEHSFDVE
EHPDHRILAT NPCGEQPLEE YEACNLGHIN LSTLAAQDAP DWRVWSQTHD FDTLEAGVSR
FLDEAMDTDA FQRRIEMGTR FLENVVTMSD FPVPEIEQKV SEMRKIGLGV MGLAQLYIQL
GVKYGSEEGN EIASQLMQTI NHDSKTASHE LALERGSFDE WDNSKFAAPT EYADWFEHHT
GEDAADWADG YPIRNHNTTT IAPTGTTSMV GNTTGGCEPI YNVAYYKNVS DDVQGDEMLV
EFDDYFLRTL EDNDIDVQAV KEEAQTQMAN NDFDGVDGLT TVPDAIGELF VVTSDLSGKD
HAAVQTACQN GVDSAISKTC NFPNDASVED MDEVYRYIYD NGGKGVTVYR DGTRSKQVLT
TRADNTEFSG LDEEEAAAAM VDTIQETFGG IEGFLENDDI QDAFGADLRE LFATGDDAAF
DEEDFAEKQP RPDLLHGVTQ RVDTGYGKLY VTINENPERE RPFELFANTG NSGGFTGSFT
EALAKTISVA LRSGVDPDEI ADKLQGIRSP KVAWDKGEQV NSIPDAFGTA LRRYLNGDVD
RAAYPQQQHL TEIDADDAAH HETDGGAAES LGGPQGPTGA GESADAQQQS QDATQSLIDA
GESPECPECG AMTLYYSEGC KTCESCGWSE C
//
