ID A0A3R9P334_9BACI Unreviewed; 353 AA.
AC A0A3R9P334;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-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 ORFNames=D7Z54_32860 {ECO:0000313|EMBL:RSL29138.1};
OS Salibacterium salarium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=284579 {ECO:0000313|EMBL:RSL29138.1, ECO:0000313|Proteomes:UP000275076};
RN [1] {ECO:0000313|EMBL:RSL29138.1, ECO:0000313|Proteomes:UP000275076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM0101 {ECO:0000313|EMBL:RSL29138.1,
RC ECO:0000313|Proteomes:UP000275076};
RA Yamprayoonswat W., Boonvisut S., Jumpathong W., Sittihan S., Ruangsuj P.,
RA Wanthongcharoen S., Thongpramul N., Pimmason S., Yu B., Yasawong M.;
RT "Draft genome sequence of Bacillus salarius IM0101, isolated from a
RT hypersaline soil in Inner Mongolia, China.";
RL Submitted (OCT-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 -!- 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:RSL29138.1}.
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DR EMBL; RBVX01000092; RSL29138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9P334; -.
DR OrthoDB; 9766544at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000275076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000355,
KW ECO:0000256|PIRSR:PIRSR000355-2};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000355,
KW ECO:0000313|EMBL:RSL29138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275076};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 96
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 126
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 129
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 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 353 AA; 40609 MW; 0C760E1198E21DE6 CRC64;
MDGRGDQPLA TLERVKILEP ENPNRSTALF GGKASGILNW NDIPYPHFYD IRKEMRALFW
IADEVDMSSD KKQFPTLPQK ERTAFLKING LLAEIDGPQT DLAARISNFS TDPSVKATFA
TEADQESEHN QSYAYVLSSV ATSDQQIASF EEGRTDPVLL RRNQRMIDIY NEFAVNPTIE
TVLRALLYTV IAEGLFFYSG FAFFYNLARN QKMLGTAKMI SFINRDELQH SKFAGELFRA
TLAENPEYNT KEFTEWIYEE FENAVEQEIE WSRYVLDGID GIDLVEMAGY VKYRANKMLR
MVGLSDIYEG YTENPMKWIR AYSDNFDDTK GDFFETDIDT YAKITELNGF DKL
//
