RIR2_ALKHC
ID RIR2_ALKHC Reviewed; 345 AA.
AC Q9KFH7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=nrdB; OrderedLocusNames=BH0502;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; BA000004; BAB04221.1; -; Genomic_DNA.
DR PIR; F83712; F83712.
DR RefSeq; WP_010896680.1; NC_002570.2.
DR PDB; 2RCC; X-ray; 1.90 A; A/B/C=1-345.
DR PDBsum; 2RCC; -.
DR AlphaFoldDB; Q9KFH7; -.
DR SMR; Q9KFH7; -.
DR STRING; 272558.10173115; -.
DR EnsemblBacteria; BAB04221; BAB04221; BAB04221.
DR KEGG; bha:BH0502; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_035339_1_0_9; -.
DR OMA; KVGEYQR; -.
DR OrthoDB; 1384440at2; -.
DR UniPathway; UPA00326; -.
DR EvolutionaryTrace; Q9KFH7; -.
DR Proteomes; UP000001258; Chromosome.
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:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 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; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..345
FT /note="Ribonucleoside-diphosphate reductase subunit beta"
FT /id="PRO_0000190468"
FT ACT_SITE 125
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:2RCC"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 105..132
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:2RCC"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 206..236
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 243..267
FT /evidence="ECO:0007829|PDB:2RCC"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:2RCC"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:2RCC"
SQ SEQUENCE 345 AA; 40242 MW; D89208F7518152BC CRC64;
MEQLQKRKIY DTTASNASTG ILNGKSSNVL NWDDVRFSWA YPLYKNMLAN FWTPFEINMS
HDAKQFPTLT ETEQEAFKKI IGLLAFLDSV QTDYSMRAAE YLTDSSLAAL MSVLSFQEVV
HNQSYSYVLS SLVPKATQDE IFEYWKHDDV LKERNEFIID GYEKFVDNPT PKTFLESIVY
DVILEGLNFY SGFAFFYNLA RNQKMVSTST MINYINRDEQ LHVYLFTNIF KELLVEFPEL
NTEETKTFVK TTLMKAADLE KDWFRYIIGD KIPGINPEDM ETYISFIANK RAVQLGMEKP
YPEIKHNPMK WIRAYEDVNS GKSDFFEQKS RQYAKVSADN GFDEL
