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Reviewed, UniProtKB/Swiss-Prot P24702 (SODC_ACTPL)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1
Gene names
Name: sodC
OrganismActinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)
Taxonomic identifier715 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

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Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

Catalytic activity

2 superoxide + 2 H+ = O2 + H2O2.

Cofactor

Binds 1 copper ion per subunit.

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the Cu-Zn superoxide dismutase family.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 190167Superoxide dismutase [Cu-Zn]
PRO_0000032817

Sites

Metal binding831Copper; catalytic
Metal binding851Copper; catalytic
Metal binding1081Copper; catalytic
Metal binding1081Zinc; structural
Metal binding1171Zinc; structural
Metal binding1261Zinc; structural
Metal binding1291Zinc; structural
Metal binding1641Copper; catalytic

Amino acid modifications

Disulfide bond90 ↔ 186

Experimental info

Sequence conflict1131E → D in AAB02816. Ref.2
Sequence conflict1241N → D in AAB02816. Ref.2
Sequence conflict134 – 1363FVE → TIA in AAB02816. Ref.2

Secondary structure

1 ................................ 190
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P24702-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 5FC1F3148972DC83

FASTA19020,207
        10         20         30         40         50         60 
MKLTNLALAF TLFGASAVAF AHADHDHKKA DNSSVEKLVV QVQQLDPVKG NKDVGTVEIT 

        70         80         90        100        110        120 
ESAYGLVFTP HLHGLAQGLH GFHIHQNPSC EPKEKDGKLV AGLGAGGHWD PKETKQHGYP 

       130        140        150        160        170        180 
WSDNAHLGDL PALFVEHDGS ATNPVLAPRL KKLDEVKGHS LMIHEGGDNH SDHPAPLGGG 

       190 
GPRMACGVIK

« Hide

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References

[1]"Cloning and molecular characterization of Cu,Zn superoxide dismutase from Actinobacillus pleuropneumoniae."
Langford P.R., Loynds B.M., Kroll J.S.
Infect. Immun. 64:5035-5041(1996) [PubMed: 8945543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Serotype III / Isolate 1421 (Nielsen).
[2]Helie M.C., Sirois M., Ouellet C., Boissinot M.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S 4074 / Serotype 1.
[3]"recF in Actinobacillus pleuropneumoniae."
Loynds B.M., Langford P.R., Kroll J.S.
Nucleic Acids Res. 20:615-615(1992) [PubMed: 1741300] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-190.
Strain: Serotype III / Isolate 1421 (Nielsen).
[4]"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] OF 91-177.
Strain: Serotype III / Isolate 1421 (Nielsen).
[5]"Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface."
Forest K.T., Langford P.R., Kroll J.S., Getzoff E.D.
J. Mol. Biol. 296:145-153(2000) [PubMed: 10656823] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

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Cross-references

Sequence databases

X99396 Genomic DNA. Translation: CAA67771.1.
U51440 Genomic DNA. Translation: AAB02816.1.
X63626 Genomic DNA. Translation: CAA45174.1.
X83123 Genomic DNA. Translation: CAA58204.1.
PIRI39650.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2APSX-ray1.90A/B29-190[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.15.1.1. 257522.

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]
ProDomPD000469. SOD_CU_ZN. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSODC_ACTPL
AccessionPrimary (citable) accession number: P24702
Secondary accession number(s): Q59135
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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