ID M9RR95_9RHOB Unreviewed; 1223 AA.
AC M9RR95;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 Name=nrdJ {ECO:0000313|EMBL:AGI72310.1};
GN ORFNames=OA238_c22320 {ECO:0000313|EMBL:AGI72310.1};
OS Octadecabacter arcticus 238.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI72310.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI72310.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI72310.1,
RC ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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; CP003742; AGI72310.1; -; Genomic_DNA.
DR RefSeq; WP_015495405.1; NC_020908.1.
DR AlphaFoldDB; M9RR95; -.
DR STRING; 391616.OA238_c22320; -.
DR KEGG; oar:OA238_c22320; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_5; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000004688; 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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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.
DR SUPFAM; SSF75625; YebC-like; 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:UP000004688}.
FT DOMAIN 31..139
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 190..738
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 813..903
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1223 AA; 133131 MW; D40AC6FD5CD1F12D CRC64;
MKIERSFTKS GQDAFAEVPF KAATSEIRNP DGTIVFKLEN CQIPIGWSQV ASDVIAQKYF
RKAGVPSETV RVAEKGVPEF LWRSVPAEGA QMSGEISAKQ VFDRLAGAWT YWGWKGGYFT
TEEDAQTYFD EMRYMLATQR AAPNSPQWFN TGLHWAYGID GPAQGHHYVD YKTGKLTASK
SSYEHPQPHA CFIQSVKDDL VNEGGIMDLW VREARLFKYG SGTGTNFSSL RASGESLSGG
GKSSGLMGFL KIGDRAAGAI KSGGTTRRAA KMVIVDADHP DIEEFINWKV LEEQKVASIV
AGSKMHEQKL NLIFDAIRTW DGKADDAYDP KVNPALKDAV REAKKVCIPE TYVKRVLDYA
RQGHTAIEFP TYDTDWDSEA YNSVSGQNSN NSIRVTDAFL KAVEDDANWK LINRKNGEVA
KVIKARDLWE QVGHAAWACA DPGIQYHDTV NAWHTCPEDG AIRGSNPCSE YMFLDDTACN
LASMNLLKFF KDGEFQVEDY MHASRLWTVT LEISVMMAQF PSKEIAQRSF DFRTLGLGYA
NIGGLLMNMG FGYDSDEGRS MAGALTAIMT GVSYATSAEI AGELGAFSGY GRNKDHMLKV
IRNHRNAAYG ASDGYEKLDI KPVPLDHANC PDARLIDIAM STWDEALRLG EKHGYRNAQV
SVIAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYFKI INQSVPAALA KLGYSTSQAE
EIQAYAVGHG TLGNAPGINH TALIGHGFGP AEIEKIEEAL PSAFDIRFVF NQWTLGEDFC
TKVLGIPADK LNDPTFDLLK SLGFSKEDAD LANDHVCGTM TLEGAPHLKE EHYVVFDCAN
PCGKTGKRYL SVNSHIYMMA AAQSFISGAI SKTINMANNA TIEDCQKAYE LSWSLGIKAN
ALYRDGSKLS QPLAAALIED DEEAADILEN GNIHAKAQVI AEKIIEKVVI KEIIKSHREK
MPQRRKGYTQ KANVGGHKVY LRTGEYEDGN LGEIFIDMHK EGAGFRAMMN NFAIAVSVGL
QYGVPLEEFV DAFTFTKFEP AGMVQGNDSI KNATSILDYI FRELAVSYLD RTDLAHVKPE
GATFDSLGRG EEEGVSNIQE MSDSAASRSL EVLKQISSTG YLRKRVPNDL YVLQGGAGAV
AFGGGDAAVA LETMIPAVAV GGGMAKATTT TAIASGAIGI TARDKAKMQG YEGEACGECG
NYTLVRNGTC MKCNTCGGTS GCS
//
