ID A0A1M6J8E9_9BACE Unreviewed; 871 AA.
AC A0A1M6J8E9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05444350_12747 {ECO:0000313|EMBL:SHJ42969.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHJ42969.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHJ42969.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHJ42969.1,
RC ECO:0000313|Proteomes:UP000184192};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZN01000027; SHJ42969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6J8E9; -.
DR eggNOG; COG0209; Bacteria.
DR Proteomes; UP000184192; Unassembled WGS sequence.
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:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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 48..112
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 130..662
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 871 AA; 98684 MW; 4A92DFF11250AC0B CRC64;
MQSHLLMIGI TSTLLLIKNK SKEKSIVEKQ TYSYDEAYEE SLRYFQGDEL AARVWVNKYA
VKDSFGNIYE KSPEDMHWRI ANEVARIEAK YSNPLSAEEL FGLLDHFKYI VPQGSPMTGI
GNNHQVASLS NCFVIGVDGE ADSYGAIFKI DEEQVQLMKR RGGVGHDLSH IRPKGSPVKN
SALTSTGLVP FMERYSNSTR EVAQDGRRGA LMLSVSIKHP DSEAFIDAKM TEGKVTGANV
SVKLDDAFMT AAITGTPYIQ QYPVYSAEPT VQKEINATNL WKKIVHNAWK SAEPGVLFWD
TILKESVPDC YADLGYRTVS TNPCGEIPLC PYDSCRLLAI NLYSYVVNPF KPDAYFDFDL
FKKHVGLAQR IMDDIIDLEL EKIERIMEKI DTDPESEDVR HTERTLWDKI YKKSGQGRRT
GVGITAEGDM LAALGLRYGT EEATEFSEKV HKTVALNAYR SSVEMAKERG AFEIYDTERE
KNNPFINRLR EADPELYEEM KKYGRRNIAC LTIAPTGTTS LMTQTTSGIE PVFLPVYKRR
RKVNPNDTNV HIDFVDDTGD AFEEYIVFHP KFVTWLEAKG YDPAKRYTQE EIDALVEQSP
YYKATSNDVD WLMKVKMQGR IQKWVDHSIS VTINLPNDVD EDLVNRLYVE AWKSGCKGCT
VYRDGSRSGV LISAKSEKKE DLPPCKPPTV VETRPRVLDA DIVRFQNNKE KWVAFVGLLD
GHPYEIFTGL QDDDEGIILP KNVTTGHIIK NVDKDGNKRY DFQFQNKRGY KVTIEGLSEK
FNKEYWNYAK LISGVLRYRM PIEQVIKLVG SLQLDSESIN TWKNGVERAL KKYITDGTEA
KGKKCPNCGN ETLVYQEGCL ICTTCGASRC G
//
