SODF3_ARATH
ID SODF3_ARATH Reviewed; 263 AA.
AC Q9FMX0; O81240; Q8LCD9;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Superoxide dismutase [Fe] 3, chloroplastic {ECO:0000303|PubMed:18996978, ECO:0000303|PubMed:9765550};
DE EC=1.15.1.1 {ECO:0000269|PubMed:18996978};
DE AltName: Full=Protein FE SUPEROXIDE DISMUTASE 3 {ECO:0000303|PubMed:18996978, ECO:0000303|PubMed:9765550};
DE Flags: Precursor;
GN Name=FSD3 {ECO:0000303|PubMed:18996978, ECO:0000303|PubMed:9765550};
GN OrderedLocusNames=At5g23310 {ECO:0000312|Araport:AT5G23310};
GN ORFNames=MKD15.17 {ECO:0000312|EMBL:BAB11186.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-262, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=9765550; DOI=10.1104/pp.118.2.637;
RA Kliebenstein D.J., Monde R.A., Last R.L.;
RT "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
RT disparate regulation and protein localization.";
RL Plant Physiol. 118:637-650(1998).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18996978; DOI=10.1105/tpc.108.061341;
RA Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T., Motohashi R.,
RA Shono Y., Nagata N., Ikeuchi M., Shinozaki K.;
RT "A heterocomplex of iron superoxide dismutases defends chloroplast
RT nucleoids against oxidative stress and is essential for chloroplast
RT development in Arabidopsis.";
RL Plant Cell 20:3148-3162(2008).
RN [7]
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=23057508; DOI=10.1111/j.1469-8137.2012.04369.x;
RA Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C., Weiss C.,
RA Azem A., Jinn T.L.;
RT "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity
RT independent of its co-chaperonin role in Arabidopsis chloroplasts.";
RL New Phytol. 197:99-110(2013).
RN [8]
RP INTERACTION WITH MRL7.
RX PubMed=23956074; DOI=10.1093/mp/sst092;
RA Yua Q.B., Ma Q., Kong M.M., Zhao T.T., Zhang X.L., Zhou Q., Huang C.,
RA Chong K., Yang Z.N.;
RT "AtECB1/MRL7, a thioredoxin-like fold protein with disulfide reductase
RT activity, regulates chloroplast gene expression and chloroplast biogenesis
RT in Arabidopsis thaliana.";
RL Mol. Plant 7:206-217(2014).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems (By
CC similarity). Plays important role in chloroplast development,
CC particularly in the maintenance of thylakoids membranes. Seems to act
CC as a heterodimer with FSD2. {ECO:0000250|UniProtKB:Q9X6W9,
CC ECO:0000269|PubMed:18996978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC Evidence={ECO:0000269|PubMed:18996978};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q9X6W9};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q9X6W9};
CC -!- ACTIVITY REGULATION: Activated by cpn20/cpn21 (in vitro).
CC {ECO:0000269|PubMed:23057508}.
CC -!- SUBUNIT: Homodimer. Heterodimer with FSD2 (PubMed:18996978). Interacts
CC with MRL7 (PubMed:23956074). {ECO:0000269|PubMed:18996978,
CC ECO:0000269|PubMed:23956074}.
CC -!- INTERACTION:
CC Q9FMX0; Q9LU64: FSD2; NbExp=7; IntAct=EBI-4430441, EBI-4424866;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid
CC {ECO:0000269|PubMed:18996978}.
CC -!- DISRUPTION PHENOTYPE: Pale green phenotype. Abnormal plastids, highly
CC vacuolated and without internal membrane structures like thylakoids.
CC {ECO:0000269|PubMed:18996978}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; AB007648; BAB11186.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93150.1; -; Genomic_DNA.
DR EMBL; AY065458; AAL38899.1; -; mRNA.
DR EMBL; AY091225; AAM14164.1; -; mRNA.
DR EMBL; AY086656; AAM63713.1; -; mRNA.
DR EMBL; AF061852; AAC24834.1; -; mRNA.
DR PIR; T51732; T51732.
DR RefSeq; NP_197722.1; NM_122237.4.
DR AlphaFoldDB; Q9FMX0; -.
DR SMR; Q9FMX0; -.
DR BioGRID; 17670; 4.
DR IntAct; Q9FMX0; 4.
DR STRING; 3702.AT5G23310.1; -.
DR PaxDb; Q9FMX0; -.
DR PRIDE; Q9FMX0; -.
DR ProMEX; Q9FMX0; -.
DR ProteomicsDB; 232600; -.
DR EnsemblPlants; AT5G23310.1; AT5G23310.1; AT5G23310.
DR GeneID; 832395; -.
DR Gramene; AT5G23310.1; AT5G23310.1; AT5G23310.
DR KEGG; ath:AT5G23310; -.
DR Araport; AT5G23310; -.
DR TAIR; locus:2166953; AT5G23310.
DR eggNOG; KOG0876; Eukaryota.
DR HOGENOM; CLU_031625_0_0_1; -.
DR InParanoid; Q9FMX0; -.
DR OMA; YLHSIFW; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; Q9FMX0; -.
DR PRO; PR:Q9FMX0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMX0; baseline and differential.
DR Genevisible; Q9FMX0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; IDA:UniProtKB.
DR GO; GO:0009534; C:chloroplast thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0042646; C:plastid nucleoid; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF46609; SSF46609; 1.
DR SUPFAM; SSF54719; SSF54719; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Iron; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..41
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 42..263
FT /note="Superoxide dismutase [Fe] 3, chloroplastic"
FT /id="PRO_0000421266"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 127
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT BINDING 215
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q9X6W9"
FT CONFLICT 227
FT /note="K -> N (in Ref. 4; AAM63713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 30360 MW; 33B1BBDEC9EF0B0C CRC64;
MSSCVVTTSC FYTISDSSIR LKSPKLLNLS NQQRRRSLRS RGGLKVEAYY GLKTPPYPLD
ALEPYMSRRT LEVHWGKHHR GYVDNLNKQL GKDDRLYGYT MEELIKATYN NGNPLPEFNN
AAQVYNHDFF WESMQPGGGD TPQKGVLEQI DKDFGSFTNF REKFTNAALT QFGSGWVWLV
LKREERRLEV VKTSNAINPL VWDDIPIICV DVWEHSYYLD YKNDRAKYIN TFLNHLVSWN
AAMSRMARAE AFVNLGEPNI PIA
