SRX_ARATH
ID SRX_ARATH Reviewed; 125 AA.
AC Q8GY89; A8MS24; Q8LC51; Q9SA12;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Sulfiredoxin, chloroplastic/mitochondrial;
DE Short=AtSRX;
DE EC=1.8.98.2;
DE Flags: Precursor;
GN Name=SRX; OrderedLocusNames=At1g31170; ORFNames=F28K20.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17217469; DOI=10.1111/j.1365-313x.2006.02969.x;
RA Rey P., Becuwe N., Barrault M.-B., Rumeau D., Havaux M., Biteau B.,
RA Toledano M.B.;
RT "The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic
RT acid reductase involved in the photooxidative stress response.";
RL Plant J. 49:505-514(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-50; LYS-62; CYS-94 AND
RP GLU-98, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=20176891; DOI=10.1093/jxb/erq016;
RA Iglesias-Baena I., Barranco-Medina S., Lazaro-Payo A.,
RA Lopez-Jaramillo F.J., Sevilla F., Lazaro J.-J.;
RT "Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys
RT peroxiredoxin.";
RL J. Exp. Bot. 61:1509-1521(2010).
RN [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-94, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21139087; DOI=10.1104/pp.110.166504;
RA Iglesias-Baena I., Barranco-Medina S., Sevilla F., Lazaro J.-J.;
RT "The dual-targeted plant sulfiredoxin retroreduces the sulfinic form of
RT atypical mitochondrial peroxiredoxin.";
RL Plant Physiol. 155:944-955(2011).
CC -!- FUNCTION: Contributes to oxidative stress resistance by reducing
CC cysteine-sulfinic acid formed under exposure to oxidants in a
CC peroxiredoxin. May catalyze the reduction in a multi-step process by
CC acting both as a specific phosphotransferase and a thioltransferase.
CC Required to switch on the antioxidant pathway to regenerate the
CC oxidative damage. In mitochondrion, catalyzes the retroreduction of the
CC inactive sulfinic form of atypical Prx IIF using thioredoxin as
CC reducing agent. {ECO:0000269|PubMed:17217469,
CC ECO:0000269|PubMed:20176891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-
CC [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-
CC L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA-
CC COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-
CC COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974,
CC ChEBI:CHEBI:456216; EC=1.8.98.2;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=79 uM for peroxiredoxin-(S-hydroxy-S-oxocysteine) (in the presence
CC of 1 mM of ATP) {ECO:0000269|PubMed:20176891};
CC KM=29 uM for ATP (in the presence of 40 uM of peroxiredoxin-(S-
CC hydroxy-S-oxocysteine)) {ECO:0000269|PubMed:20176891};
CC Note=kcat is 0.66 min(-1) with peroxiredoxin-(S-hydroxy-S-
CC oxocysteine) as substrate (in the presence of 1 mM of ATP) and 0.025
CC min(-1) with ATP as substrate (in the presence of 40 uM of
CC peroxiredoxin-(S-hydroxy-S-oxocysteine)).;
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:20176891};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q8GY89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GY89-2; Sequence=VSP_044416;
CC -!- TISSUE SPECIFICITY: Low expression in photosynthetic tissues such as
CC leaves and sepals. {ECO:0000269|PubMed:17217469}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of overoxidized peroxiredoxin (Prx)
CC and hyperoxidized form of Prx IIF, especially in response to
CC photooxidative stress, H(2)O(2) treatment and water deficit. Increased
CC tolerance to photooxidative stress generated by high light combined
CC with low temperature. In long days, smaller leaves.
CC {ECO:0000269|PubMed:17217469, ECO:0000269|PubMed:20176891,
CC ECO:0000269|PubMed:21139087}.
CC -!- SIMILARITY: Belongs to the sulfiredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004793; AAD21682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31321.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31322.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31323.1; -; Genomic_DNA.
DR EMBL; AK117789; BAC42435.1; -; mRNA.
DR EMBL; BT004731; AAO42977.1; -; mRNA.
DR EMBL; AY086792; AAM63841.1; -; mRNA.
DR PIR; F86437; F86437.
DR RefSeq; NP_001077637.1; NM_001084168.1. [Q8GY89-1]
DR RefSeq; NP_001077638.1; NM_001084169.1. [Q8GY89-2]
DR RefSeq; NP_564375.1; NM_102855.4. [Q8GY89-1]
DR PDB; 6KY4; X-ray; 3.20 A; A=23-125.
DR PDBsum; 6KY4; -.
DR AlphaFoldDB; Q8GY89; -.
DR SMR; Q8GY89; -.
DR BioGRID; 25239; 1.
DR STRING; 3702.AT1G31170.4; -.
DR PaxDb; Q8GY89; -.
DR PRIDE; Q8GY89; -.
DR ProteomicsDB; 228382; -. [Q8GY89-1]
DR EnsemblPlants; AT1G31170.1; AT1G31170.1; AT1G31170. [Q8GY89-1]
DR EnsemblPlants; AT1G31170.2; AT1G31170.2; AT1G31170. [Q8GY89-1]
DR EnsemblPlants; AT1G31170.3; AT1G31170.3; AT1G31170. [Q8GY89-2]
DR GeneID; 840004; -.
DR Gramene; AT1G31170.1; AT1G31170.1; AT1G31170. [Q8GY89-1]
DR Gramene; AT1G31170.2; AT1G31170.2; AT1G31170. [Q8GY89-1]
DR Gramene; AT1G31170.3; AT1G31170.3; AT1G31170. [Q8GY89-2]
DR KEGG; ath:AT1G31170; -.
DR Araport; AT1G31170; -.
DR eggNOG; KOG3388; Eukaryota.
DR HOGENOM; CLU_124532_3_0_1; -.
DR InParanoid; Q8GY89; -.
DR OMA; SDELMIH; -.
DR PhylomeDB; Q8GY89; -.
DR BRENDA; 1.8.98.2; 399.
DR PRO; PR:Q8GY89; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GY89; baseline and differential.
DR Genevisible; Q8GY89; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0032542; F:sulfiredoxin activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR016692; Sulfiredoxin.
DR PANTHER; PTHR21348; PTHR21348; 1.
DR Pfam; PF02195; ParBc; 1.
DR PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antioxidant; ATP-binding; Chloroplast;
KW Disulfide bond; Mitochondrion; Nucleotide-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..125
FT /note="Sulfiredoxin, chloroplastic/mitochondrial"
FT /id="PRO_0000420170"
FT DISULFID 94
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 77..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044416"
FT MUTAGEN 50
FT /note="R->Q: Reduced activity. Loss of activity; when
FT associated with A-98."
FT /evidence="ECO:0000269|PubMed:20176891"
FT MUTAGEN 62
FT /note="K->Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:20176891"
FT MUTAGEN 94
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20176891,
FT ECO:0000269|PubMed:21139087"
FT MUTAGEN 98
FT /note="E->A: No phenotype. Loss of activity; when
FT associated with Q-50."
FT /evidence="ECO:0000269|PubMed:20176891"
FT CONFLICT 56
FT /note="R -> K (in Ref. 5; AAM63841)"
FT /evidence="ECO:0000305"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6KY4"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6KY4"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6KY4"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:6KY4"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6KY4"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6KY4"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6KY4"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:6KY4"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:6KY4"
SQ SEQUENCE 125 AA; 13914 MW; BD6AAC1C8BCA3615 CRC64;
MANLMMRLPI SLRSFSVSAS SSNGSPPVIG GSSGGVGPMI VELPLEKIRR PLMRTRSNDQ
NKVKELMDSI RQIGLQVPID VIEVDGTYYG FSGCHRYEAH QKLGLPTIRC KIRKGTKETL
RHHLR
