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P82205 (SODC_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1
OrganismBombyx mori (Silk moth)
Taxonomic identifier7091 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. UniProtKB P00441

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2. UniProtKB P00441

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity UniProtKB P00441.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164080

Sites

Metal binding451Copper; catalytic By similarity UniProtKB P00441
Metal binding471Copper; catalytic By similarity UniProtKB P00441
Metal binding621Copper; catalytic By similarity UniProtKB P00441
Metal binding621Zinc; structural By similarity
Metal binding701Zinc; structural By similarity UniProtKB P00441
Metal binding791Zinc; structural By similarity UniProtKB P00441
Metal binding821Zinc; structural By similarity UniProtKB P00441
Metal binding1201Copper; catalytic By similarity UniProtKB P00441

Amino acid modifications

Disulfide bond56 ↔ 146 By similarity UniProtKB P00441

Secondary structure

1 ............... 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82205 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 174BF407D1820775

FASTA15415,842
        10         20         30         40         50         60 
MPAKAVCVLR GDVSGTVFFD QQDEKSPVVV SGEVQGLTKG KHGFHVHEFG DNTNGCTSAG 

        70         80         90        100        110        120 
AHFNPEKQDH GGPSSAVRHV GDLGNIEAIE DSGVTKVSIQ DSQISLHGPN SIIGRTLVVH 

       130        140        150 
ADPDDLGLGG HELSKTTGNA GGRIACGVIG LAKI

« Hide

References

[1]"Cu/Zn superoxide dismutase in Bombyx mori."
Hong S.M., Kang S.W., Kim N.S., Lee J.S., Nho S.K.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Kl20.
[2]"Protein database for several tissues derived from five instar of silkworm."
Zhong B.-X.
Yi Chuan Xue Bao 28:217-224(2001) [PubMed: 11280994] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31.
Strain: Xinhang X Keming.
Tissue: Body wall and Fat body.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY461705 mRNA. Translation: AAR97568.1.
RefSeqNP_001037084.1. NM_001043619.1.
UniGeneBmo.328.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L9EX-ray2.05A/B/C/D1-154[»]
3L9YX-ray1.80A/B1-154[»]
ProteinModelPortalP82205.
SMRP82205. Positions 4-153.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID692639.

Organism-specific databases

CTD39251.

Phylogenomic databases

OMATQEGDGP.
OrthoDBEOG43TXBZ.
PhylomeDBP82205.

Family and domain databases

InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_BOMMO
AccessionPrimary (citable) accession number: P82205
Secondary accession number(s): Q6SA03
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 59 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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