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Protein

Superoxide dismutase [Fe] 2, chloroplastic

Gene

FSD2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD3.By similarity1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Enzyme regulationi

Activated by cpn20/cpn21 (in vitro).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi77 – 771IronBy similarity
Metal bindingi129 – 1291IronBy similarity
Metal bindingi228 – 2281IronBy similarity
Metal bindingi232 – 2321IronBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
  • removal of superoxide radicals Source: GOC
  • response to UV Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Fe] 2, chloroplastic (EC:1.15.1.1)
Alternative name(s):
Protein ALBINO OR PALE GREEN 8
Protein FE SUPEROXIDE DISMUTASE 2
Gene namesi
Name:FSD2
Synonyms:APG8
Ordered Locus Names:At5g51100
ORF Names:MWD22.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G51100.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast nucleoid Source: UniProtKB
  • chloroplast thylakoid Source: UniProtKB-SubCell
  • nucleoid Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Pale green phenotype. Abnormal plastids, highly vacuolated and without internal membrane structures like thylakoids.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646ChloroplastSequence analysisAdd
BLAST
Chaini47 – 305259Superoxide dismutase [Fe] 2, chloroplasticPRO_0000421265Add
BLAST

Proteomic databases

PaxDbiQ9LU64.
PRIDEiQ9LU64.

PTM databases

iPTMnetiQ9LU64.

Expressioni

Inductioni

By UV-B treatment. Induced by salt stress.2 Publications

Gene expression databases

GenevisibleiQ9LU64. AT.

Interactioni

Subunit structurei

Heterodimer with FSD3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FSD3Q9FMX07EBI-4424866,EBI-4430441

Protein-protein interaction databases

BioGridi20428. 9 interactions.
IntActiQ9LU64. 8 interactions.
STRINGi3702.AT5G51100.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LU64.
SMRiQ9LU64. Positions 49-268.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiQ9LU64.
KOiK04564.
OMAiYINTFME.
PhylomeDBiQ9LU64.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LU64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNVAVTATP SSLLYSPLLL PSQGPNRRMQ WKRNGKRRLG TKVAVSGVIT
60 70 80 90 100
AGFELKPPPY PLDALEPHMS RETLDYHWGK HHKTYVENLN KQILGTDLDA
110 120 130 140 150
LSLEEVVLLS YNKGNMLPAF NNAAQAWNHE FFWESIQPGG GGKPTGELLR
160 170 180 190 200
LIERDFGSFE EFLERFKSAA ASNFGSGWTW LAYKANRLDV ANAVNPLPKE
210 220 230 240 250
EDKKLVIVKT PNAVNPLVWD YSPLLTIDTW EHAYYLDFEN RRAEYINTFM
260 270 280 290 300
EKLVSWETVS TRLESAIARA VQREQEGTET EDEENPDDEV PEVYLDSDID

VSEVD
Length:305
Mass (Da):34,664
Last modified:October 1, 2000 - v1
Checksum:i6A68EAF701EA5AC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023044 Genomic DNA. Translation: BAA97372.1.
CP002688 Genomic DNA. Translation: AED96034.1.
BT004073 mRNA. Translation: AAO42100.1.
BT005116 mRNA. Translation: AAO50649.1.
AK228538 mRNA. Translation: BAF00460.1.
AY085077 mRNA. Translation: AAM61633.1.
Y12641 mRNA. Translation: CAA73188.1.
RefSeqiNP_199923.1. NM_124489.2.
UniGeneiAt.212.

Genome annotation databases

EnsemblPlantsiAT5G51100.1; AT5G51100.1; AT5G51100.
GeneIDi835183.
GrameneiAT5G51100.1; AT5G51100.1; AT5G51100.
KEGGiath:AT5G51100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023044 Genomic DNA. Translation: BAA97372.1.
CP002688 Genomic DNA. Translation: AED96034.1.
BT004073 mRNA. Translation: AAO42100.1.
BT005116 mRNA. Translation: AAO50649.1.
AK228538 mRNA. Translation: BAF00460.1.
AY085077 mRNA. Translation: AAM61633.1.
Y12641 mRNA. Translation: CAA73188.1.
RefSeqiNP_199923.1. NM_124489.2.
UniGeneiAt.212.

3D structure databases

ProteinModelPortaliQ9LU64.
SMRiQ9LU64. Positions 49-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20428. 9 interactions.
IntActiQ9LU64. 8 interactions.
STRINGi3702.AT5G51100.1.

PTM databases

iPTMnetiQ9LU64.

Proteomic databases

PaxDbiQ9LU64.
PRIDEiQ9LU64.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G51100.1; AT5G51100.1; AT5G51100.
GeneIDi835183.
GrameneiAT5G51100.1; AT5G51100.1; AT5G51100.
KEGGiath:AT5G51100.

Organism-specific databases

TAIRiAT5G51100.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiQ9LU64.
KOiK04564.
OMAiYINTFME.
PhylomeDBiQ9LU64.

Miscellaneous databases

PROiQ9LU64.

Gene expression databases

GenevisibleiQ9LU64. AT.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Van Breusegem F., Villaroel R., Van Montagu M., Inze D.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-305.
    Strain: cv. Columbia.
  7. "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization."
    Kliebenstein D.J., Monde R.A., Last R.L.
    Plant Physiol. 118:637-650(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY UV-B, GENE FAMILY.
  8. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
    Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
    Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. "Long-term effects of mild salt stress on growth, ion accumulation and superoxide dismutase expression of Arabidopsis rosette leaves."
    Attia H., Arnaud N., Karray N., Lachaal M.
    Physiol. Plantarum 132:293-305(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY SALT.
  10. "A heterocomplex of iron superoxide dismutases defends chloroplast nucleoids against oxidative stress and is essential for chloroplast development in Arabidopsis."
    Myouga F., Hosoda C., Umezawa T., Iizumi H., Kuromori T., Motohashi R., Shono Y., Nagata N., Ikeuchi M., Shinozaki K.
    Plant Cell 20:3148-3162(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION.
  11. "CHAPERONIN 20 mediates iron superoxide dismutase (FeSOD) activity independent of its co-chaperonin role in Arabidopsis chloroplasts."
    Kuo W.Y., Huang C.H., Liu A.C., Cheng C.P., Li S.H., Chang W.C., Weiss C., Azem A., Jinn T.L.
    New Phytol. 197:99-110(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiSODF2_ARATH
AccessioniPrimary (citable) accession number: Q9LU64
Secondary accession number(s): O04879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.