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Database: UniProt
Entry: Q9FMX0
LinkDB: Q9FMX0
Original site: Q9FMX0 
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   16-JAN-2019, entry version 120.
DE   RecName: Full=Superoxide dismutase [Fe] 3, chloroplastic;
DE            EC=1.15.1.1;
DE   AltName: Full=Protein FE SUPEROXIDE DISMUTASE 3;
DE   Flags: Precursor;
GN   Name=FSD3; OrderedLocusNames=At5g23310; ORFNames=MKD15.17;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.
RT   Sequence features of the regions of 1,191,918 bp covered by seventeen
RT   physically 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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=18996978; DOI=10.1105/tpc.108.061341;
RA   Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T.,
RA   Motohashi R., 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.
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.,
RA   Weiss C., 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
RT   biogenesis 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
CC       systems (By similarity). Plays important role in chloroplast
CC       development, particularly in the maintenance of thylakoids
CC       membranes. Seems to act as a heterodimer with FSD2. {ECO:0000250,
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   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by cpn20/cpn21 (in vitro).
CC       {ECO:0000269|PubMed:23057508}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with FSD2 (PubMed:18996978).
CC       Interacts with MRL7 (PubMed:23956074).
CC       {ECO:0000269|PubMed:18996978, ECO:0000269|PubMed:23956074}.
CC   -!- INTERACTION:
CC       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,
CC       highly vacuolated and without internal membrane structures like
CC       thylakoids. {ECO:0000269|PubMed:18996978}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
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   UniGene; At.28472; -.
DR   ProteinModelPortal; 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   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   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013584; -.
DR   InParanoid; Q9FMX0; -.
DR   KO; K04564; -.
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:0009295; C:nucleoid; IDA:TAIR.
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   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 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   PIRSF; PIRSF000349; SODismutase; 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; Complete proteome; Iron; Metal-binding; Oxidoreductase;
KW   Plastid; Reference proteome; Thylakoid; Transit peptide.
FT   TRANSIT       1     41       Chloroplast. {ECO:0000255}.
FT   CHAIN        42    263       Superoxide dismutase [Fe] 3,
FT                                chloroplastic.
FT                                /FTId=PRO_0000421266.
FT   METAL        74     74       Iron. {ECO:0000250}.
FT   METAL       127    127       Iron. {ECO:0000250}.
FT   METAL       211    211       Iron. {ECO:0000250}.
FT   METAL       215    215       Iron. {ECO:0000250}.
FT   CONFLICT    227    227       K -> N (in Ref. 4; AAM63713).
FT                                {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
//
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