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Protein

Superoxide dismutase [Cu-Zn]

Gene

sodC

Organism
Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Copper; catalytic
Metal bindingi85 – 851Copper; catalytic
Metal bindingi108 – 1081Copper; catalytic
Metal bindingi108 – 1081Zinc; structural
Metal bindingi117 – 1171Zinc; structural
Metal bindingi126 – 1261Zinc; structural
Metal bindingi129 – 1291Zinc; structural
Metal bindingi164 – 1641Copper; catalytic

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:sodC
OrganismiActinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)
Taxonomic identifieri715 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 190167Superoxide dismutase [Cu-Zn]PRO_0000032817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi90 ↔ 186

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi228399.Aple02000411.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 446Combined sources
Beta strandi47 – 493Combined sources
Beta strandi52 – 6211Combined sources
Beta strandi65 – 728Combined sources
Beta strandi77 – 804Combined sources
Beta strandi82 – 887Combined sources
Beta strandi93 – 953Combined sources
Beta strandi98 – 1003Combined sources
Helixi103 – 1053Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi145 – 1473Combined sources
Helixi153 – 1564Combined sources
Beta strandi159 – 1668Combined sources
Beta strandi170 – 1756Combined sources
Helixi176 – 1794Combined sources
Beta strandi182 – 1898Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2APSX-ray1.90A/B29-190[»]
ProteinModelPortaliP24702.
SMRiP24702. Positions 36-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24702.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLTNLALAF TLFGASAVAF AHADHDHKKA DNSSVEKLVV QVQQLDPVKG
60 70 80 90 100
NKDVGTVEIT ESAYGLVFTP HLHGLAQGLH GFHIHQNPSC EPKEKDGKLV
110 120 130 140 150
AGLGAGGHWD PKETKQHGYP WSDNAHLGDL PALFVEHDGS ATNPVLAPRL
160 170 180 190
KKLDEVKGHS LMIHEGGDNH SDHPAPLGGG GPRMACGVIK
Length:190
Mass (Da):20,207
Last modified:November 1, 1997 - v2
Checksum:i5FC1F3148972DC83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131E → D in AAB02816 (Ref. 2) Curated
Sequence conflicti124 – 1241N → D in AAB02816 (Ref. 2) Curated
Sequence conflicti134 – 1363FVE → TIA in AAB02816 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99396 Genomic DNA. Translation: CAA67771.1.
U51440 Genomic DNA. Translation: AAB02816.1.
X63626 Genomic DNA. Translation: CAA45174.1.
X83123 Genomic DNA. Translation: CAA58204.1.
PIRiI39650.

Genome annotation databases

GeneIDi4850277.
PATRICi41507603. VBIActPle54414203709_0019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99396 Genomic DNA. Translation: CAA67771.1.
U51440 Genomic DNA. Translation: AAB02816.1.
X63626 Genomic DNA. Translation: CAA45174.1.
X83123 Genomic DNA. Translation: CAA58204.1.
PIRiI39650.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2APSX-ray1.90A/B29-190[»]
ProteinModelPortaliP24702.
SMRiP24702. Positions 36-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi228399.Aple02000411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4850277.
PATRICi41507603. VBIActPle54414203709_0019.

Phylogenomic databases

eggNOGiENOG4108Z7T. Bacteria.
COG2032. LUCA.

Miscellaneous databases

EvolutionaryTraceiP24702.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiSODC_ACTPL
AccessioniPrimary (citable) accession number: P24702
Secondary accession number(s): Q59135
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 1, 1997
Last modified: November 11, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.