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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD

Organism
Schistosoma mansoni (Blood fluke)
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 bindingi45Copper; catalytic1
Metal bindingi47Copper; catalytic1
Metal bindingi62Copper; catalytic1
Metal bindingi62Zinc; structural1 Publication1
Metal bindingi70Zinc; structural1 Publication1
Metal bindingi79Zinc; structural1 Publication1
Metal bindingi82Zinc; structural1 Publication1
Metal bindingi119Copper; 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:SOD
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001641051 – 153Superoxide dismutase [Cu-Zn]Add BLAST153

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 145

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi6183.Smp_176200.2__mRNA.

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi10 – 12Combined sources3
Beta strandi14 – 23Combined sources10
Beta strandi28 – 36Combined sources9
Beta strandi39 – 48Combined sources10
Turni53 – 56Combined sources4
Helixi57 – 59Combined sources3
Beta strandi76 – 78Combined sources3
Beta strandi82 – 88Combined sources7
Beta strandi94 – 102Combined sources9
Beta strandi104 – 106Combined sources3
Helixi107 – 109Combined sources3
Beta strandi114 – 121Combined sources8
Helixi133 – 136Combined sources4
Beta strandi141 – 147Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TO4X-ray1.55A/B/C/D1-153[»]
1TO5X-ray2.20A/B/C/D1-153[»]
ProteinModelPortaliQ01137.
SMRiQ01137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01137.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
OrthoDBiEOG091G0OG2.

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]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01137-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAVCVMTGT AGVKGVVKFT QETDNGPVHV HAEFSGLKAG KHGFHVHEFG
60 70 80 90 100
DTTNGCTSAG AHFNPTKQEH GAPEDSIRHV GDLGNVVAGA DGNAVYNATD
110 120 130 140 150
KLISLNGSHS IIGRTMVIHE NEDDLGRGGH ELSKVTGNAG GRLACGVIGL

AAE
Length:153
Mass (Da):15,721
Last modified:April 1, 1993 - v1
Checksum:iD30014FDBD34593A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115T → S in AAA29935 (PubMed:1426133).Curated1
Sequence conflicti148I → V (PubMed:1426133).Curated1
Sequence conflicti148I → V (PubMed:7895835).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86867 mRNA. Translation: AAA29936.1.
M97298 mRNA. Translation: AAA29935.1.
L12159, L12008, L12158 Genomic DNA. Translation: AAC14467.1.
PIRiA49241.

Genome annotation databases

GeneDBiSmp_176200.1:pep.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86867 mRNA. Translation: AAA29936.1.
M97298 mRNA. Translation: AAA29935.1.
L12159, L12008, L12158 Genomic DNA. Translation: AAC14467.1.
PIRiA49241.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TO4X-ray1.55A/B/C/D1-153[»]
1TO5X-ray2.20A/B/C/D1-153[»]
ProteinModelPortaliQ01137.
SMRiQ01137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_176200.2__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiSmp_176200.1:pep.

Phylogenomic databases

eggNOGiKOG0441. Eukaryota.
COG2032. LUCA.
HOGENOMiHOG000263447.
OrthoDBiEOG091G0OG2.

Miscellaneous databases

EvolutionaryTraceiQ01137.

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]
PRINTSiPR00068. CUZNDISMTASE.
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_SCHMA
AccessioniPrimary (citable) accession number: Q01137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.