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Q59081 (SODC_AGGAC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name:sodC
OrganismAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifier714 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Protein attributes

Sequence length87 AA.
Sequence statusFragment.
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

Homodimer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
Gene Ontology (GO)
   Biological processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

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

Chain‹1 – ›87›87Superoxide dismutase [Cu-Zn]
PRO_0000164160

Sites

Metal binding181Copper; catalytic By similarity
Metal binding181Zinc; structural By similarity
Metal binding271Zinc; structural By similarity
Metal binding361Zinc; structural By similarity
Metal binding391Zinc; structural By similarity
Metal binding741Copper; catalytic By similarity

Experimental info

Non-terminal residue11
Non-terminal residue871

Sequences

Sequence LengthMass (Da)Tools
Q59081 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6704173D25976550

FASTA879,287
        10         20         30         40         50         60 
EPKEKDGKLT AGLGAGGHWD PKDTKQHGYP WQDDAHLGDL PALTVLHDGT AANPVLAPRI 

        70         80 
KHLDDVRGHS LMIHAGGDNH SDHPAPL 

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References

[1]"Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!"
Kroll J.S., Langford P.R., Wilks K.E., Keil A.D.
Microbiology 141:2271-2279(1995) [PubMed: 7496539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43718 / FDC Y4 / Serotype b.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83122 Genomic DNA. Translation: CAA58203.1.
PIRI39485.

3D structure databases

ProteinModelPortalQ59081.
SMRQ59081. Positions 1-87.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. Partial match.
PS00332. SOD_CU_ZN_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_AGGAC
AccessionPrimary (citable) accession number: Q59081
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 27, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families