ID A0A0U3PGN0_9ACTN Unreviewed; 968 AA.
AC A0A0U3PGN0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AS200_13030 {ECO:0000313|EMBL:ALV32870.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32870.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV32870.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32870.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013743; ALV32870.1; -; Genomic_DNA.
DR RefSeq; WP_058922548.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PGN0; -.
DR STRING; 1725411.AS200_13030; -.
DR KEGG; scx:AS200_13030; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000068029; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 56..139
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 160..699
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 105673 MW; D90DDA8026E24295 CRC64;
MTETASGPAR SSRAKGTKAA ANKGLRIERI HTTPGVHPYD EVNWERRDVV MTNWRDGSVN
FEQRGVEFPD FWSVNAVNIV TSKYFRGAVG TPQRETGLKQ LIDRIVKTYR KAGEDYKYFA
SPADAEIFEH ELAYALLHQI FSFNSPVWFN VGTPQPQQVS ACFILSVDDS MESILDWYKE
EGMIFKGGSG AGLNLSRIRS SKELLSSGGN ASGPVSFMRG ADASAGTIKS GGATRRAAKM
VILDVDHPDI EDFIETKVKE EEKIRALRDA GFDMDLGGDD ITSVQYQNAN NSVRVNDEFM
KAVEQGGKFG LRARMTGEVI EEVEAKVLFR KMAEAAWACA DPGIQYDDTI NRWHTCPESG
RINGSNPCSE YMHLDNTSCN LASLNLMKFL KDDGKGHQSF EVERFAKVVE LVITAMDISI
CFADFPTQKI GENTRAFRQL GIGYANLGAL LMATGHAYDS DGGRALAGAI TSLMTGTSYK
RSAELAAVVG AYDGYARNAT AHNRVMKQHA DANTGAVRVD DLDTPIWAAA TEAWQDVLRL
GEKNGFRNSQ ASVIAPTGTI GLAMSCDTTG LEPDLALVKF KKLVGGGSMQ IVNGTVPQAL
RRLGYQEEQI EAIVAHIAEH GNVIDAPGLK HEHYEVFDCA MGERSISAMG HVRMMAAIQP
WISGALSKTV NLPESATVED VEEVYFEAWK MGVKALAIYR DNCKVGQPLS AKTKEKEKAE
VTEKAEATIR ETVEKVIEYR PVRKRLPKGR PGITTSFTVG GAEGYMTANS YPDDGLGEVF
LKMSKQGSTL AGMMDAFSIA VSVGLQYGVP LETYVSKFTN MRFEPAGMTD DPDVRMAQSI
VDYIFRRLAL DFLPFETRSA LGIHSAEERQ RHLETGSYEQ SLDEDEVDVE GLAQSAPRAQ
ELKAVATPRA EVEAAKPAPK QAHTSAELVE MQLGIQADAP LCFSCGTKMQ RAGSCYICEG
CGSTSGCS
//
