ID A4EQE3_9RHOB Unreviewed; 765 AA.
AC A4EQE3;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=RSK20926_13219 {ECO:0000313|EMBL:EBA18685.1};
OS Roseobacter sp. SK209-2-6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA18685.1, ECO:0000313|Proteomes:UP000005964};
RN [1] {ECO:0000313|EMBL:EBA18685.1, ECO:0000313|Proteomes:UP000005964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA18685.1,
RC ECO:0000313|Proteomes:UP000005964};
RA Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA18685.1}.
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DR EMBL; AAYC01000001; EBA18685.1; -; Genomic_DNA.
DR RefSeq; WP_008204242.1; NZ_AAYC01000001.1.
DR AlphaFoldDB; A4EQE3; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000005964; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005964}.
FT DOMAIN 8..80
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..552
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 765 AA; 83945 MW; 2D3D6EB09C4FD79A CRC64;
MSRFAAPIAE QIWDMKYRFK QADGTPIDVT VEDSWRRIAR DLARAEQDPE AWEGKFYEAL
EDFKYLPAGR ITAGAGTARQ VTLFNCFVMG TVPDSMGGIF DMLKEAALTM QQGGGIGYDF
STIRPRGADV KGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEQFIT
AKSDPARLRM FNMSVLVTDD FMEAVKADGS WELQFGGKVY HTVEARDLWN KIMQATYDFA
EPGVIFIDRI NKANNLSYVE DICATNPCGE QPLPPYGACL LGSINMARLV SNPFEKNAGL
NQEAMQELVA TAVRMMDNVV DVSKFPLEAQ AQEAQNKRRI GLGVTGLADA LLMLGLEYGS
DEAARQTDEW LHGIARAAYL ASVELAKEKG AFPLFDADAY LASGNMLNMD EDVREAIRTH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYTRKVL QKDGSRTEEE VVDYAVQMYR
EKFGADAKLP GFFVNAQTLS PAAHVKMQAA AQKWIDSSIS KTINCPEDIS FDDFKDVYMQ
AWDQGCKGCT TYRPNDVTGS VLTVSENADT APGETAQAPH DSGSDANGAE VVYMSEPLDR
PQSLEGHTYK LKWPDSEHAI YLTINDIIIN GHRRPFEVFI NSKNMEHYAW TLALTRMISA
VFRRGGDVSF VVEELKAVFD PRGGAWVQGK YIPSILAAIG GVIETHMVKT GFLEGEGMGL
KSDPQAEVVN LNAPRGKPCP SCGQYDLQMV EGCMTCRSCG HSKCG
//
