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Reviewed, UniProtKB/Swiss-Prot P0AGD2 (SODC_ECO57)

Last modified December 15, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1
Alternative name(s):
    Bacteriocuprein
Gene names
Name: sodC
Ordered Locus Names: Z2661, ECs2355
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionantioxidant activity

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 173154Superoxide dismutase [Cu-Zn]
PRO_0000045306

Sites

Metal binding671Copper; catalytic By similarity
Metal binding691Copper; catalytic By similarity
Metal binding921Copper; catalytic By similarity
Metal binding921Zinc; structural By similarity
Metal binding1011Zinc; structural By similarity
Metal binding1091Zinc; structural By similarity
Metal binding1121Zinc; structural By similarity
Metal binding1471Copper; catalytic By similarity

Amino acid modifications

Disulfide bond74 ↔ 169 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AGD2-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 9A0CB65F03AAB197

FASTA17317,681
        10         20         30         40         50         60 
MKRFSLAILA LVVATGAQAA SEKVEMNLVT SQGVGQSIGS VTITETDKGL EFSPDLKALP 

        70         80         90        100        110        120 
PGEHGFHIHA KGSCQPATKD GKASAAESAG GHLDPQNTGK HEGPEGAGHL GDLPALVVNN 

       130        140        150        160        170 
DGKATDAVIA PRLKSLDEIK DKALMVHVGG DNMSDQPKPL GGGGERYACG VIK 

« Hide

References

Cross-references

Sequence databases

AE005174 Genomic DNA. Translation: AAG56635.1.
BA000007 Genomic DNA. Translation: BAB35778.1.
PIRC90923.
G85771.
RefSeqNP_288082.1.
NP_310382.1.

3D structure databases

SMRP0AGD2. Positions 20-173.
ModBaseSearch...

Genome annotation databases

GeneID914926.
961605.
GenomeReviewsGene locus Z2661 in contig AE005174_GR.
Gene locus ECs2355 in contig BA000007_GR.
KEGGece:Z2661.
ecs:ECs2355.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG609879.
OMAHGFHLHA.

Enzyme and pathway databases

BioCycECOL83334:ECS2355-MON.

Family and domain databases

InterProIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[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]
PROSITEPS00087. SOD_CU_ZN_1. False negative.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_ECO57
AccessionPrimary (citable) accession number: P0AGD2
Secondary accession number(s): P53635, P96756
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: December 15, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents