ID A0A1G9RAD8_9SPHI Unreviewed; 1105 AA.
AC A0A1G9RAD8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05421813_107156 {ECO:0000313|EMBL:SDM19817.1};
OS Daejeonella rubra.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=990371 {ECO:0000313|EMBL:SDM19817.1, ECO:0000313|Proteomes:UP000199226};
RN [1] {ECO:0000313|Proteomes:UP000199226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24536 {ECO:0000313|Proteomes:UP000199226};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNHH01000007; SDM19817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9RAD8; -.
DR STRING; 990371.SAMN05421813_107156; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000199226; Unassembled WGS sequence.
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; -; 2.
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; 2.
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:UP000199226}.
FT DOMAIN 48..135
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 186..667
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 734..830
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1105 AA; 121369 MW; 11B7FAE90CE57A7E CRC64;
MGKSSTKPAA KGTGKGLGFQ RYFTKEGVNV YDLFNYEKRT SVIRNPAGDA VFEMKNVEVP
DSWSQVATDI LAQKYFRKAG VPQPDGTTSS ENSIKQVAHR MAHCWQSWGE RYNYFASKED
ASIFYDELVY TIVGQLAAPN SPQWFNTGLH SSYGITGKPQ GHYFVNPDTD QLEKSTSAYE
RPQPHACFIL SVSDDLVNDG GIMDLWVREA RIFKYGSGVG TNFSAIRGES EKLSGGGYSS
GLMSFLKIGD RAAGAIKSGG TTRRAAKMVC LDLEHPEIEN FVNWKVEEEK KVAALIAAGY
SSDYEGEAYR TVSGQNSNNS VRVPNTFFKA LEEGGNWDLI GRISGKPVKS ISAEKLWQDI
SFAAWACADP GIQYDTTINE WHTCPEGGRI NASNPCSEYM FLDNTACNLA SINLAHFFDP
QTLVFDVKGF EHACRVWTVV LEISVLMAQF PSKEVAQLSY DYRTLGLGYA NLGSMLMVAG
IPYDSDKARA IGGAITAIMT GTAYSTSAEM AKELGTFKKF EENKKHMLRV MRNHRYAAYN
NDAYEGLEIA PPGIDPKYCP DYLLSAACNS WDKAVELGEK YGYRNAQTTV IAPTGTIGLV
MDCDTTGIEP DFALVKFKKL SGGGYFKIIN QGVPAALRNQ GYKEHEIEAI VNYAKGAATL
EGAPHINFDS LAAKGFTQDE LEKIDKSLLA AFEIGFVFNQ WSLGEECLNR LGFKSEQYSS
PDFNLLRSIG FNRQQIAEAN EFICGTMTVE GAPYLKEEHY QIFDCANKCG QKGERYIHAH
GHIKMMAAAQ PFLSGAISKT VNLPNEATVE EIKDCYELSW KLALKANALY RDGCKLSQPL
STKSSDSKED KLDTVEEVLG QAANVKLSDL TADQVLEAAR AILERSTDTK FKRQLSSVVE
RKNLPGKRGG FTQKAAVGGQ TVFVRTGQYE DGTLGEIFVD MHKEGATFRS LMNCFSIAVS
VGLQYGVPLE EFVDKFTFTR FEPSGMVSGH DNIKSATSIV DYIFRMLGYE YLNRTDLVHV
LTEQKVILGN PQMTDEDVNT DTTNTFAEKP VSVSTSTSGL KLKPVLDISG GGQSDAPACG
NCGHIMVRSG TCYKCLNCGT QGGCS
//
