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Entry: A0A371QSJ1_9BACT
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ID   A0A371QSJ1_9BACT        Unreviewed;       326 AA.
AC   A0A371QSJ1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE            EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN   ORFNames=DYD21_02425 {ECO:0000313|EMBL:REL38828.1};
OS   Rhodohalobacter sp. SW132.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC   Rhodohalobacter.
OX   NCBI_TaxID=2293433 {ECO:0000313|EMBL:REL38828.1, ECO:0000313|Proteomes:UP000263328};
RN   [1] {ECO:0000313|EMBL:REL38828.1, ECO:0000313|Proteomes:UP000263328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW132 {ECO:0000313|EMBL:REL38828.1,
RC   ECO:0000313|Proteomes:UP000263328};
RA   Song L.;
RT   "Rhodohalobacter alkaliphilus sp. nov.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:REL38828.1}.
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DR   EMBL; QUOK01000001; REL38828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371QSJ1; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000263328; 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   Reference proteome {ECO:0000313|Proteomes:UP000263328}.
FT   BINDING         72
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         176
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         210
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ   SEQUENCE   326 AA;  37824 MW;  A5B06E89CB1EA1AC CRC64;
     MKLTGKTSVR ENIKLTEDPS YPIFKELYEK QKKAIWFPEE LNIQQDALDY QSLSENEKDL
     FDTAVGYFCS SELLVQNVLV NTFFPLLTDP HAKMSFSTQL FMENIHSDFF EIVLQSFGMD
     RDKMYEVAFE DPILRKKQSL IVDAIDKISQ DGIDPDTIAG QKQILKAILL NNIVMEGIFF
     YSSFAHFFAL KDMGKMNNVV SGVELVLIDE SLHLQNGIEA ILIMLDENPE ITEDEAFVNE
     IRDLILEGAE LEIEYVEHKF GDHTILGISF GELERYLKYI TDRRLQELGF EPEFHITENP
     LRFLQKEDVK KLINFFEVSS TEYTNY
//
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