ID RIR2_DICDI Reviewed; 338 AA. AC P42521; Q556I9; Q86AN2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 27-MAR-2024, entry version 148. DE RecName: Full=Ribonucleoside-diphosphate reductase small subunit; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase small subunit; GN Name=rnrB-1; Synonyms=nrdB; ORFNames=DDB_G0272616; GN and GN Name=rnrB-2; Synonyms=nrdB; ORFNames=DDB_G0274021; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE. RX PubMed=8950185; DOI=10.1016/s0167-4781(96)00109-1; RA Tsang A., Bonfils C., Czaika G., Shtevi A., Grant C.; RT "A prespore-specific gene of Dictyostelium discoideum encodes the small RT subunit of ribonucleotide reductase."; RL Biochim. Biophys. Acta 1309:100-108(1996). RN [2] RP SEQUENCE REVISION TO 233-237. RA Tsang A.; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=12097910; DOI=10.1038/nature00847; RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., RA Noegel A.A.; RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; RL Nature 418:79-85(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10014}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 2 iron ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Heterodimer of a large and a small subunit. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expression is detected in growing cells and CC decreases dramatically at the onset of development. The rnrB transcript CC reappears after the cells have formed multicellular aggregates. CC {ECO:0000269|PubMed:8950185}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000305}. CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and CC AX4. These strains contain a duplication of a segment of 750 kb of CC chromosome 2 compared to the corresponding sequence in strain AX2. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L36941; AAB72227.2; -; Genomic_DNA. DR EMBL; AAFI02000011; EAL70444.1; -; Genomic_DNA. DR EMBL; AAFI02000009; EAL70945.1; -; Genomic_DNA. DR RefSeq; XP_644369.1; XM_639277.1. DR RefSeq; XP_645045.1; XM_639953.1. DR AlphaFoldDB; P42521; -. DR SMR; P42521; -. DR STRING; 44689.P42521; -. DR PaxDb; 44689-DDB0185062; -. DR EnsemblProtists; EAL70444; EAL70444; DDB_G0274021. DR EnsemblProtists; EAL70945; EAL70945; DDB_G0272616. DR GeneID; 8618721; -. DR GeneID; 8619255; -. DR KEGG; ddi:DDB_G0272616; -. DR KEGG; ddi:DDB_G0274021; -. DR dictyBase; DDB_G0272616; rnrB-1. DR dictyBase; DDB_G0274021; rnrB-2. DR eggNOG; KOG1567; Eukaryota. DR HOGENOM; CLU_035339_2_1_1; -. DR InParanoid; P42521; -. DR OMA; KVGEYQR; -. DR PhylomeDB; P42521; -. DR PRO; PR:P42521; -. DR Proteomes; UP000002195; Chromosome 2. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:dictyBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:dictyBase. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:dictyBase. DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase. 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; IPR030475; RNR_small_AS. 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. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Deoxyribonucleotide synthesis; Iron; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..338 FT /note="Ribonucleoside-diphosphate reductase small subunit" FT /id="PRO_0000190456" FT ACT_SITE 119 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 81 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 112 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 112 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 115 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 174 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 208 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 211 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 338 AA; 39371 MW; 9BF33B855246CD3B CRC64; MEEINKKDTF IEPILKENKD RFVLFPIKYP DIWRMYKKAL ASHWVAEEID LGNDNVDWEY KLTDNERHFI SHVLAFFAAS DGIVNENLAT RFMSEVQIPE ARCFYGFQIA IENIHSETYS LLIETYIKDK QTKDKLFNAI ETIPCIKKKA EWALRWINDS DSFAERLVAF AAVEGIFFSG SFCSIFWLKK RGLMQGLTFS NELISRDEGL HCDFACLLYT KLQRKLDPKV IEKMIRDAVE CEKEFICESL PVDLIGMNSR SMSQYIEFCA DRLVVSLGYK KIFNSSNPFE WMEMISLQRK SNFFEGKVAE YAKTGVAIQG NNQQKNNQSR TLVLDEDF //