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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)DescriptionActionsGraphical viewLength
Metal bindingi83Copper; catalytic1
Metal bindingi85Copper; catalytic1
Metal bindingi108Copper; catalytic1
Metal bindingi108Zinc; structural1
Metal bindingi117Zinc; structural1
Metal bindingi126Zinc; structural1
Metal bindingi129Zinc; structural1
Metal bindingi164Copper; catalytic1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Add BLAST23
ChainiPRO_000003281724 – 190Superoxide dismutase [Cu-Zn]Add BLAST167

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi90 ↔ 186

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi228399.Aple02000411.

Structurei

Secondary structure

1190
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 44Combined sources6
Beta strandi47 – 49Combined sources3
Beta strandi52 – 62Combined sources11
Beta strandi65 – 72Combined sources8
Beta strandi77 – 80Combined sources4
Beta strandi82 – 88Combined sources7
Beta strandi93 – 95Combined sources3
Beta strandi98 – 100Combined sources3
Helixi103 – 105Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi145 – 147Combined sources3
Helixi153 – 156Combined sources4
Beta strandi159 – 166Combined sources8
Beta strandi170 – 175Combined sources6
Helixi176 – 179Combined sources4
Beta strandi182 – 189Combined sources8

3D structure databases

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

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti113E → D in AAB02816 (Ref. 2) Curated1
Sequence conflicti124N → D in AAB02816 (Ref. 2) Curated1
Sequence conflicti134 – 136FVE → TIA in AAB02816 (Ref. 2) Curated3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2APSX-ray1.90A/B29-190[»]
ProteinModelPortaliP24702.
SMRiP24702.
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

CDDicd00305. Cu-Zn_Superoxide_Dismutase. 1 hit.
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...

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 2, 2016
This is version 107 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.