ID V9XIH1_9NOCA Unreviewed; 927 AA.
AC V9XIH1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=Y013_10300 {ECO:0000313|EMBL:AHD21042.1}, Y013_14420
GN {ECO:0000313|EMBL:AHD21770.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD21770.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD21770.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD21770.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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|ARBA:ARBA00025437, 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; CP006996; AHD21042.1; -; Genomic_DNA.
DR EMBL; CP006996; AHD21770.1; -; Genomic_DNA.
DR AlphaFoldDB; V9XIH1; -.
DR KEGG; rpy:Y013_10300; -.
DR KEGG; rpy:Y013_14420; -.
DR PATRIC; fig|1435356.3.peg.2065; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_11; -.
DR Proteomes; UP000018781; 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 CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 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|ARBA:ARBA00022634,
KW 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 53..133
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 155..689
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 839..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 99496 MW; 33655BDA72E45BDF CRC64;
MSSTRPHSSP KSASDAAAAA VRGDVRYFTT PGVDPAEAVE WQRRDARIVH HGTGRVVFEQ
TDVEFPAFWS QNATDIVTQK YFRGQLGHPD REHSLRDVIA RIVDTITAWG HTDGHLDDPE
AFAAELTYLL IHQRASFNSP VWFNIGVPNT PQQASACFIL SVDDSIDSIL EWYRQEAVIF
KGGSGAGVNL SRIRSSAEPL TGGGSASGPV SFMRGADASA GTIKSGGKTR RAAKMVILDV
DHPDIEEFVD CKAIEERKAR VLAEAGFDMG LDGTDIHSVQ YQNANNSVRV TDEFMHAVVA
DAEWPLRTVT TGETVRTVRA RELLQRTAAA TWECADPGIQ YDTTINAWHT ASATGRINAS
NPCSEYMHLD DSACNLASLN LLTFLREDGT FDVDGFRHSV AVMLTAQEIL VGRADYPTER
IGETSRRFRQ LGLGYANLGA LLMASGLPYD SEAGRATAAA ITALMTGHAY AVSADMARRL
GPFDGFDENR APMLDVLGKH RGALDDIDAD LAPADVLDAA RQAWDRAVAD GSAHGVRNSQ
VSVLAPTGTI GLAMDCDTTG IEPDLALVKT KKLVGGGSLT IVNRSVPRAL SRLGYSPSEV
ADIVAHLDLH HDLAGAPHVR DEHAPVFATS MGDNVISPRG HVAMMAAVQP FLSGAISKTV
NLPESATVDD IADMYVDAWR LGVKALAIYR DNCKLGQPLS TASRPAVAEA APSTAPRRER
LPRTRTSRTF EFRVADCKGF VTIGEYDDGR PGEMFLRVSK QGSTLAGIMD AFSMSVSYGL
QYGVPLRTFV RAFTSTRFEP AGITDDPDLR IATSILDYIF RRLAIDYLEP DERAELGILT
GAERSVPDTP TLTPYTSTPP VREPDPPATA PRGTHSTSSA STSSPGGLAA PSPSNPDAPY
CMQCGVKMQR AGSCHACPSC GNTSGCS
//
