ID A0A443IRJ5_9RHOB Unreviewed; 324 AA.
AC A0A443IRJ5; A0A443JT41;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN Name=nrdF {ECO:0000313|EMBL:RWR08905.1};
GN ORFNames=D2T30_04155 {ECO:0000313|EMBL:RWR23646.1}, D2T33_15215
GN {ECO:0000313|EMBL:RWR08905.1};
OS Sinirhodobacter populi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Sinirhodobacter.
OX NCBI_TaxID=2306993 {ECO:0000313|EMBL:RWR08905.1, ECO:0000313|Proteomes:UP000285710};
RN [1] {ECO:0000313|Proteomes:UP000284476, ECO:0000313|Proteomes:UP000285710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2D-5 {ECO:0000313|EMBL:RWR08905.1,
RC ECO:0000313|Proteomes:UP000285710}, and SK2B-1
RC {ECO:0000313|EMBL:RWR23646.1, ECO:0000313|Proteomes:UP000284476};
RA Xu G.;
RT "Sinorhodobacter populi sp. nov. isolated from the symptomatic bark tissue
RT of Populus euramericana canker.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000284476, ECO:0000313|Proteomes:UP000285710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2D-5 {ECO:0000313|EMBL:RWR08905.1,
RC ECO:0000313|Proteomes:UP000285710}, and SK2B-1
RC {ECO:0000313|EMBL:RWR23646.1, ECO:0000313|Proteomes:UP000284476};
RA Li Y.;
RL Submitted (JAN-2019) 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 -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
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:RWR08905.1}.
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DR EMBL; SAUW01000016; RWR08905.1; -; Genomic_DNA.
DR EMBL; SAUZ01000003; RWR23646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443IRJ5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000284476; Unassembled WGS sequence.
DR Proteomes; UP000285710; Unassembled WGS sequence.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro.
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 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; IPR026494; RNR_NrdF-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR NCBIfam; TIGR04171; RNR_1b_NrdF; 1.
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.
DR PROSITE; PS00368; RIBORED_SMALL; 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:RWR08905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285710}.
FT ACT_SITE 110
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
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 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 324 AA; 36938 MW; 0E2BB61B277CD5FF CRC64;
MKDHAVSKTV LKAINWNRLQ DDKDLEVWNR LTANFWLPEK VPLSNDVPSW ATLRPEEQTL
TIRVFTGLTL LDTVQNNVGA PSLMPDSITP HEEAVLSNIA FMEAVHARSY SSIFSTLCGM
KEVDEAFRWS EENPHLQAKA QIVLDKYRAT EHPLKKKVAS VFLESFLFYS GFYLPMYWSS
RAKLTNTADL IRLIIRDEAV HGYYIGYKYQ RGLETLSEAQ RQEMKDFAFS LIFDLYEIET
KYTEELYDGI GLTEDVKAFL HYNANKALQN LGYEALFPPQ ACEVNPAILA ALSPDSENHD
FFSGSGSSYV IGKAVATEDE DWDF
//
