ID REHYB_ORYSJ Reviewed; 220 AA.
AC P0C5D1; A2YP42; B7ELX7; Q8GVG9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=1-Cys peroxiredoxin B;
DE Short=1-Cys Prx B;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Thioredoxin peroxidase B;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin B {ECO:0000305};
GN OrderedLocusNames=Os07g0638400, LOC_Os07g44440;
GN ORFNames=OJ1340_C08.108, OsJ_024298;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively (By similarity). Seems to contribute to the inhibition of
CC germination during stress (By similarity).
CC {ECO:0000250|UniProtKB:O04005, ECO:0000250|UniProtKB:P30041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O04005}. Cytoplasm
CC {ECO:0000250|UniProtKB:O04005}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {ECO:0000250|UniProtKB:O35244}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000305}.
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DR EMBL; AP005292; BAC45198.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF22322.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT02839.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ40815.1; -; Genomic_DNA.
DR EMBL; AK073273; BAG93374.1; -; mRNA.
DR EMBL; AK104089; BAG96405.1; -; mRNA.
DR RefSeq; XP_015645187.1; XM_015789701.1.
DR AlphaFoldDB; P0C5D1; -.
DR SMR; P0C5D1; -.
DR STRING; 39947.P0C5D1; -.
DR PeroxiBase; 4024; Os1CysPrx02.
DR PaxDb; 39947-P0C5D1; -.
DR EnsemblPlants; Os07t0638400-01; Os07t0638400-01; Os07g0638400.
DR GeneID; 4344046; -.
DR Gramene; Os07t0638400-01; Os07t0638400-01; Os07g0638400.
DR KEGG; osa:4344046; -.
DR eggNOG; KOG0854; Eukaryota.
DR HOGENOM; CLU_042529_4_1_1; -.
DR InParanoid; P0C5D1; -.
DR OMA; RLTMLYP; -.
DR OrthoDB; 103042at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; P0C5D1; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Direct protein sequencing; Nucleus; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..220
FT /note="1-Cys peroxiredoxin B"
FT /id="PRO_0000285103"
FT DOMAIN 4..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 195..218
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30041"
SQ SEQUENCE 220 AA; 24233 MW; 81052C2053D893F0 CRC64;
MPGLTLGDVV PDLELDTTHG KIRLHDFVGD AYVIIFSHPA DFTPVCTTEL SEMAGYAGEF
DKRGVKLLGF SCDDVESHKD WIKDIEAYKP GRRVGFPIVA DPDREAIRQL NMIDADEKDT
AGGELPNRAL HIVGPDKKVK LSFLFPACTG RNMAEVLRAT DALLTAARHR VATPVNWKPG
ERVVIPPGVS DEEAKARFPA GFETAQLPSN KCYLRFTQVD
//
