BAS1_ORYSJ
ID BAS1_ORYSJ Reviewed; 261 AA.
AC Q6ER94; B7EFL3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=2-Cys peroxiredoxin BAS1, chloroplastic;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q96291};
DE AltName: Full=Thiol-specific antioxidant protein;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin BAS1 {ECO:0000305};
DE Flags: Precursor;
GN Name=BAS1; OrderedLocusNames=Os02g0537700, LOC_Os02g33450;
GN ORFNames=OsJ_07037 {ECO:0000312|EMBL:EEE57135.1}, OSJNBa0014M17.2,
GN P0508B05.23;
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 [MRNA], FUNCTION, AND MUTAGENESIS OF CYS-114.
RC STRAIN=cv. Nipponbare; TISSUE=Leaf;
RX PubMed=16891402; DOI=10.1105/tpc.106.041541;
RA Perez-Ruiz J.M., Spinola M.C., Kirchsteiger K., Moreno J., Sahrawy M.,
RA Cejudo F.J.;
RT "Rice NTRC is a high-efficiency redox system for chloroplast protection
RT against oxidative damage.";
RL Plant Cell 18:2356-2368(2006).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 61-67, AND IDENTIFICATION BY
RP MASS 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).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH NTRC.
RX PubMed=19345687; DOI=10.1016/j.febslet.2009.03.067;
RA Perez-Ruiz J.M., Cejudo F.J.;
RT "A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an
RT enzyme with protein disulfide reductase activity.";
RL FEBS Lett. 583:1399-1402(2009).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides (PubMed:16891402, PubMed:19345687). May be an
CC antioxidant enzyme particularly in the developing shoot and
CC photosynthesizing leaf (By similarity). {ECO:0000250|UniProtKB:Q96291,
CC ECO:0000269|PubMed:16891402, ECO:0000269|PubMed:19345687}.
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:Q96291};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By similarity).
CC Interacts with the plastidial NADPH-dependent thioredoxin reductase
CC NTRC (PubMed:19345687). {ECO:0000250|UniProtKB:Q06830,
CC ECO:0000269|PubMed:19345687}.
CC -!- INTERACTION:
CC Q6ER94; Q70G58: Os07g0657900; NbExp=5; IntAct=EBI-6956385, EBI-6956411;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q96291}.
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 typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:Q96291}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AM039889; CAJ01693.1; -; mRNA.
DR EMBL; AP004753; BAD27915.1; -; Genomic_DNA.
DR EMBL; AP005609; BAD28826.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF08964.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79077.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57135.1; -; Genomic_DNA.
DR EMBL; AK068919; BAG91160.1; -; mRNA.
DR EMBL; AK104703; BAG96892.1; -; mRNA.
DR RefSeq; XP_015627405.1; XM_015771919.1.
DR AlphaFoldDB; Q6ER94; -.
DR SMR; Q6ER94; -.
DR IntAct; Q6ER94; 2.
DR MINT; Q6ER94; -.
DR STRING; 4530.OS02T0537700-01; -.
DR PeroxiBase; 4022; Os2CysPrx01.
DR PaxDb; Q6ER94; -.
DR PRIDE; Q6ER94; -.
DR EnsemblPlants; Os02t0537700-01; Os02t0537700-01; Os02g0537700.
DR GeneID; 4329578; -.
DR Gramene; Os02t0537700-01; Os02t0537700-01; Os02g0537700.
DR KEGG; osa:4329578; -.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q6ER94; -.
DR OMA; CPLGWKP; -.
DR OrthoDB; 1326484at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ER94; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
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 SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Chloroplast; Direct protein sequencing; Disulfide bond;
KW Hydrogen peroxide; Oxidoreductase; Peroxidase; Plastid;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16758443"
FT CHAIN 61..261
FT /note="2-Cys peroxiredoxin BAS1, chloroplastic"
FT /id="PRO_0000284084"
FT DOMAIN 68..227
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 114
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 114
FT /note="Interchain (with C-236); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT DISULFID 236
FT /note="Interchain (with C-114); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q06830"
FT MUTAGEN 114
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16891402"
SQ SEQUENCE 261 AA; 28097 MW; 5F0CA432FDA0007B CRC64;
MAACCSSLAT AVSSSSAKPL AGIPPAAPHS LSLPRAPAAR PLRLSASSSR SARASSFVAR
AGGVDDAPLV GNKAPDFDAE AVFDQEFINV KLSDYIGKKY VILFFYPLDF TFVCPTEITA
FSDRYDEFEK LNTEILGVSI DSVFSHLAWV QTDRKSGGLG DLKYPLISDV TKSISKSFGV
LIPDQGIALR GLFIIDKEGV IQHSTINNLA IGRSVDETMR TLQALQYVQD NPDEVCPAGW
KPGDKSMKPD PKGSKEYFAA I
