ID E0DGZ4_9CORY Unreviewed; 330 AA.
AC E0DGZ4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN ORFNames=HMPREF0299_7149 {ECO:0000313|EMBL:EFM48896.1};
OS Corynebacterium matruchotii ATCC 14266.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM48896.1, ECO:0000313|Proteomes:UP000004218};
RN [1] {ECO:0000313|EMBL:EFM48896.1, ECO:0000313|Proteomes:UP000004218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM48896.1,
RC ECO:0000313|Proteomes:UP000004218};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM48896.1}.
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DR EMBL; ACSH02000005; EFM48896.1; -; Genomic_DNA.
DR RefSeq; WP_005526194.1; NZ_ACSH02000005.1.
DR AlphaFoldDB; E0DGZ4; -.
DR STRING; 553207.HMPREF0299_7149; -.
DR GeneID; 84574576; -.
DR eggNOG; COG0208; Bacteria.
DR OrthoDB; 9766544at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004218; 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:EFM48896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004218}.
FT ACT_SITE 116
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 206
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 330 AA; 37796 MW; 1F26B2BC6278117F CRC64;
MLNSDEDQYL ATHKEPVHAV NWNTIPDEKD LEVWDRLTGN FWLPEKVPVS NDLKSWSTLN
ELEKQTTMRV FTGLTLLDTI QGTVGAVSML PDAVTLHEEA VLTNIAFMES VHAKSYSNIF
MTLASTKEIN EAFRWSEENE NLQKKAKIIL TYYDGADPLK RKVASTLLES FLFYSGFYLP
MYWSSHAKLT NTADIIRLII RDEAVHGYYI GYKFQQALAK ESPARQEELK EYTFDVLYEL
YENEIAYTED LYDPLGWTED VKRFLRYNAN KALNNLGYEA LFPADECQVS PAILSALSPN
ADENHDFFSG SGSSYVIGKA ENTTDEDWDF
//
