ID Q87ND3_VIBPA Unreviewed; 377 AA.
AC Q87ND3;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN OrderedLocusNames=VP1935 {ECO:0000313|EMBL:BAC60198.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC60198.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC60198.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; BA000031; BAC60198.1; -; Genomic_DNA.
DR RefSeq; NP_798314.1; NC_004603.1.
DR RefSeq; WP_005457864.1; NC_004603.1.
DR AlphaFoldDB; Q87ND3; -.
DR GeneID; 1189442; -.
DR KEGG; vpa:VP1935; -.
DR PATRIC; fig|223926.6.peg.1850; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_062403_0_0_6; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000002493; Chromosome 1.
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 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 SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002493}.
SQ SEQUENCE 377 AA; 43715 MW; 7DF40F7AA562453A CRC64;
MAYSTFNQNK NDQLKEPMFL GQSVNVARYD QQKFEIFEKL IEKQLSFFWR PEEVDVSSDR
IDYNKLPDHE KHIFISNLKY QTLLDSIQGR SPNVALLPLV SLPELETWIE TWSFSETIHS
RSYTHIIRNI VNDPSVVFDD IVENEHILKR AKDIAHYYDD LIQTTNDYHR YGEGEHVLNG
ETVKVSLYDL KKKLYICLMS VNALEAIRFY VSFACSFAFA ERELMEGNAK IIKLIARDEA
LHLNGTQHMI NLLRNGQDDF SFMQIAEEAK QDCFDLFKEA AEQEKEWAEY LFKDGSMIGL
NKDILSQYVE YITNIRMQAV GLPAAYPEAT TNPIPWINAW LSSDNVQVAP QEAEISSYLV
GQIDNEVRAD DFEGFEL
//
