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Database: UniProt
Entry: B8KSN1_9GAMM
LinkDB: B8KSN1_9GAMM
Original site: B8KSN1_9GAMM 
ID   B8KSN1_9GAMM            Unreviewed;       421 AA.
AC   B8KSN1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   ORFNames=NOR51B_1397 {ECO:0000313|EMBL:EED35452.1};
OS   Luminiphilus syltensis NOR5-1B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Luminiphilus.
OX   NCBI_TaxID=565045 {ECO:0000313|EMBL:EED35452.1, ECO:0000313|Proteomes:UP000004699};
RN   [1] {ECO:0000313|Proteomes:UP000004699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX   PubMed=23705883;
RA   Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT   "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT   OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT   syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT   Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT   halotolerans.";
RL   BMC Microbiol. 13:118-118(2013).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|PIRNR:PIRNR000355}.
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|PIRNR:PIRNR000355};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000355,
CC         ECO:0000256|PIRSR:PIRSR000355-2};
CC       Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRNR:PIRNR000355,
CC       ECO:0000256|PIRSR:PIRSR000355-2};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|PIRNR:PIRNR000355}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303,
CC       ECO:0000256|PIRNR:PIRNR000355}.
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DR   EMBL; DS999411; EED35452.1; -; Genomic_DNA.
DR   RefSeq; WP_009020198.1; NZ_DS999411.1.
DR   AlphaFoldDB; B8KSN1; -.
DR   STRING; 565045.NOR51B_1397; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_035339_1_1_6; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000004699; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion 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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   PIRSF; PIRSF000355; NrdB; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|PIRNR:PIRNR000355};
KW   Iron {ECO:0000256|PIRNR:PIRNR000355, ECO:0000256|PIRSR:PIRSR000355-2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000256|PIRSR:PIRSR000355-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355,
KW   ECO:0000313|EMBL:EED35452.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004699}.
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         193
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         196
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         300
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         303
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ   SEQUENCE   421 AA;  47796 MW;  6B5AAFDDBAD918F0 CRC64;
     MLNWDDYHEE DGGNNAADIA PAVVEKTLDT ITQAEAIDDG AASVSTATPE AQDPMASEAI
     RKAAEAVASL DVAPGLEELE MGAQRVSVDE KAMINCRADL NQLVPFKYDW AWQKYIDGCA
     NHWMPQEVNM TADVATWKSS DGLTEDERRI VLRSLGYFST ADSLVANNLV LGIYRLITNP
     ECRQYLLRQA FEEAIHTHAY QYCIESLGMD EGAVFNMYRE VPSVARKATW SLSHTHSLSD
     PNFKTGTVET DQQLLRNLVG FYCVTEGIFF YCGFTQILSM GRRNKMTGVA EQFQYILRDE
     SMHLNFGIDV INQIKLENPH LWTAEFQEEV VQMILEGTQL EIEYARDTMP RGVLGMNAAM
     MEEYLQFICN RRLNQLGLSE QYPGVQNPFP WMSEIMDLRK EKNFFETRVI EYQTGGALTW
     D
//
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