Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Superoxide dismutase [Fe] 3, chloroplastic

Gene

FSD3

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 FSD2.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 bindingi74 – 741IronBy similarity
Metal bindingi127 – 1271IronBy similarity
Metal bindingi211 – 2111IronBy similarity
Metal bindingi215 – 2151IronBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Fe] 3, chloroplastic (EC:1.15.1.1)
Alternative name(s):
Protein FE SUPEROXIDE DISMUTASE 3
Gene namesi
Name:FSD3
Ordered Locus Names:At5g23310
ORF Names:MKD15.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G23310.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast nucleoid Source: UniProtKB
  • chloroplast thylakoid Source: UniProtKB-SubCell
  • nucleoid Source: TAIR
  • plastid 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 – 4141ChloroplastSequence analysisAdd
BLAST
Chaini42 – 263222Superoxide dismutase [Fe] 3, chloroplasticPRO_0000421266Add
BLAST

Proteomic databases

PaxDbiQ9FMX0.
PRIDEiQ9FMX0.
ProMEXiQ9FMX0.

Expressioni

Gene expression databases

GenevisibleiQ9FMX0. AT.

Interactioni

Subunit structurei

Homodimer. Heterodimer with FSD2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FSD2Q9LU647EBI-4430441,EBI-4424866

Protein-protein interaction databases

BioGridi17670. 4 interactions.
IntActiQ9FMX0. 4 interactions.
STRINGi3702.AT5G23310.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FMX0.
SMRiQ9FMX0. Positions 45-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiQ9FMX0.
KOiK04564.
OMAiEPNIPIA.
PhylomeDBiQ9FMX0.

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.

Q9FMX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSCVVTTSC FYTISDSSIR LKSPKLLNLS NQQRRRSLRS RGGLKVEAYY
60 70 80 90 100
GLKTPPYPLD ALEPYMSRRT LEVHWGKHHR GYVDNLNKQL GKDDRLYGYT
110 120 130 140 150
MEELIKATYN NGNPLPEFNN AAQVYNHDFF WESMQPGGGD TPQKGVLEQI
160 170 180 190 200
DKDFGSFTNF REKFTNAALT QFGSGWVWLV LKREERRLEV VKTSNAINPL
210 220 230 240 250
VWDDIPIICV DVWEHSYYLD YKNDRAKYIN TFLNHLVSWN AAMSRMARAE
260
AFVNLGEPNI PIA
Length:263
Mass (Da):30,360
Last modified:March 1, 2001 - v1
Checksum:i33B1BBDEC9EF0B0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2271K → N in AAM63713 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007648 Genomic DNA. Translation: BAB11186.1.
CP002688 Genomic DNA. Translation: AED93150.1.
AY065458 mRNA. Translation: AAL38899.1.
AY091225 mRNA. Translation: AAM14164.1.
AY086656 mRNA. Translation: AAM63713.1.
AF061852 mRNA. Translation: AAC24834.1.
PIRiT51732.
RefSeqiNP_197722.1. NM_122237.3.
UniGeneiAt.28472.

Genome annotation databases

EnsemblPlantsiAT5G23310.1; AT5G23310.1; AT5G23310.
GeneIDi832395.
GrameneiAT5G23310.1; AT5G23310.1; AT5G23310.
KEGGiath:AT5G23310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007648 Genomic DNA. Translation: BAB11186.1.
CP002688 Genomic DNA. Translation: AED93150.1.
AY065458 mRNA. Translation: AAL38899.1.
AY091225 mRNA. Translation: AAM14164.1.
AY086656 mRNA. Translation: AAM63713.1.
AF061852 mRNA. Translation: AAC24834.1.
PIRiT51732.
RefSeqiNP_197722.1. NM_122237.3.
UniGeneiAt.28472.

3D structure databases

ProteinModelPortaliQ9FMX0.
SMRiQ9FMX0. Positions 45-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17670. 4 interactions.
IntActiQ9FMX0. 4 interactions.
STRINGi3702.AT5G23310.1.

Proteomic databases

PaxDbiQ9FMX0.
PRIDEiQ9FMX0.
ProMEXiQ9FMX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G23310.1; AT5G23310.1; AT5G23310.
GeneIDi832395.
GrameneiAT5G23310.1; AT5G23310.1; AT5G23310.
KEGGiath:AT5G23310.

Organism-specific databases

TAIRiAT5G23310.

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
HOGENOMiHOG000013584.
InParanoidiQ9FMX0.
KOiK04564.
OMAiEPNIPIA.
PhylomeDBiQ9FMX0.

Miscellaneous databases

PROiQ9FMX0.

Gene expression databases

GenevisibleiQ9FMX0. 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. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [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. "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].
  5. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-262, GENE FAMILY.
    Strain: cv. Columbia.
  6. "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.
  7. "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 nameiSODF3_ARATH
AccessioniPrimary (citable) accession number: Q9FMX0
Secondary accession number(s): O81240, Q8LCD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 106 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.