REHYA_ORYSI
ID REHYA_ORYSI Reviewed; 220 AA.
AC P0C5C8; A2YP41; A3BMM5; B8B525; P52573; Q0D4A2; Q8GVH0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=1-Cys peroxiredoxin A;
DE Short=1-Cys Prx A;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Protein RAB24;
DE AltName: Full=Rice 1Cys-peroxiredoxin;
DE Short=R1C-Prx;
DE AltName: Full=Thioredoxin peroxidase A;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin A {ECO:0000305};
GN ORFNames=OsI_27030;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=17522955; DOI=10.1007/s11103-007-9174-7;
RA Liu X., Lu T., Yu S., Li Y., Huang Y., Huang T., Zhang L., Zhu J., Zhao Q.,
RA Fan D., Mu J., Shangguan Y., Feng Q., Guan J., Ying K., Zhang Y., Lin Z.,
RA Sun Z., Qian Q., Lu Y., Han B.;
RT "A collection of 10,096 indica rice full-length cDNAs reveals highly
RT expressed sequence divergence between Oryza sativa indica and japonica
RT subspecies.";
RL Plant Mol. Biol. 65:403-415(2007).
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}.
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; CM000132; EEC82522.1; -; Genomic_DNA.
DR EMBL; CT830870; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C5C8; -.
DR SMR; P0C5C8; -.
DR STRING; 39946.P0C5C8; -.
DR Allergome; 9884; Ory s 32.
DR PeroxiBase; 5148; Osi1CysPrx01.
DR CarbonylDB; P0C5C8; -.
DR EnsemblPlants; BGIOSGA026225-TA; BGIOSGA026225-PA; BGIOSGA026225.
DR Gramene; BGIOSGA026225-TA; BGIOSGA026225-PA; BGIOSGA026225.
DR HOGENOM; CLU_042529_4_1_1; -.
DR OMA; MIDYQDT; -.
DR Proteomes; UP000007015; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 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 Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Nucleus; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome; Stress response.
FT CHAIN 1..220
FT /note="1-Cys peroxiredoxin A"
FT /id="PRO_0000300260"
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; 24072 MW; 317D9D76C7D63F1D CRC64;
MPGLTIGDTV PNLELDSTHG KIRIHDFVGD TYIILFSHPG DFTPVCTTEL AAMAGYAKEF
DKRGVKLLGI SCDDVQSHKD WIKDIEAYKP GNRVTYPIMA DPSREAIKQL NMVDPDEKDS
NGGHLPSRAL HIVGPDKKVK LSFLYPSCVG RNMDEVVRAV DALQTAAKHA VATPVNWKPG
ERVVIPPGVS DDEAKEKFPQ GFDTADLPSG KGYLRFTKVG
