ID A0A419SNJ6_9BACL Unreviewed; 322 AA.
AC A0A419SNJ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta {ECO:0000256|PIRNR:PIRNR000355};
DE EC=1.17.4.1 {ECO:0000256|PIRNR:PIRNR000355};
GN ORFNames=BEP19_02570 {ECO:0000313|EMBL:RKD25837.1};
OS Ammoniphilus oxalaticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Ammoniphilus.
OX NCBI_TaxID=66863 {ECO:0000313|EMBL:RKD25837.1, ECO:0000313|Proteomes:UP000284219};
RN [1] {ECO:0000313|EMBL:RKD25837.1, ECO:0000313|Proteomes:UP000284219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAOx-1 {ECO:0000313|EMBL:RKD25837.1,
RC ECO:0000313|Proteomes:UP000284219};
RA Poppleton D.I., Gribaldo S.;
RT "Novel Firmicute Genomes.";
RL Submitted (AUG-2016) 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 -!- 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:RKD25837.1}.
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DR EMBL; MCHY01000006; RKD25837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419SNJ6; -.
DR OrthoDB; 9766544at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000284219; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000284219};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 67
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 322 AA; 37261 MW; 7A2CE91F3AE26DEA CRC64;
MTKAVYTAAN WSQHDDSFTQ LFYTQNTRQF WLPEEISLTG DIHSWKSLTD EERRAYMQVL
AGLTMLDTIQ GDDGMTSIVQ HVEGHQRKAV LTFMAAMENA VHAKSYSNIF MTLASKEEID
GLFRWVQVNP YLQRKAGMIR NYYDNITDQE SLYKAMVMSV FLESFLFYSG FYYPLYFYGQ
GRMMNSGEII NLIIRDESIH GVYVGLLAQE LYGKFSAEKQ EELKDFVFRS LQELYENEVE
YTSDVYDPVG LSSDVKVFVR YNANKALANL GFDSYFEDEE VNPVVLNGLS TETKSHDFFS
QKGNGYKKAN IEPIKDEDFI FE
//