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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionAntioxidant, Oxidoreductase
LigandCopper, 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

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

Proteomic databases

PRIDEiQ01137

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
KOiK04565
OrthoDBiEOG091G0OG2

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit

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
RefSeqiXP_018646947.1, XM_018795564.1

Genome annotation databases

GeneDBiSmp_176200.1:pep
GeneIDi8341912
KEGGismm:Smp_176200.1

Similar proteinsi

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
RefSeqiXP_018646947.1, XM_018795564.1

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...

Proteomic databases

PRIDEiQ01137

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiSmp_176200.1:pep
GeneIDi8341912
KEGGismm:Smp_176200.1

Organism-specific databases

CTDi8341912

Phylogenomic databases

eggNOGiKOG0441 Eukaryota
COG2032 LUCA
HOGENOMiHOG000263447
KOiK04565
OrthoDBiEOG091G0OG2

Miscellaneous databases

EvolutionaryTraceiQ01137

Family and domain databases

CDDicd00305 Cu-Zn_Superoxide_Dismutase, 1 hit
Gene3Di2.60.40.200, 1 hit
InterProiView protein in InterPro
IPR036423 SOD-like_Cu/Zn_dom_sf
IPR024134 SOD_Cu/Zn_/chaperone
IPR018152 SOD_Cu/Zn_BS
IPR001424 SOD_Cu_Zn_dom
PANTHERiPTHR10003 PTHR10003, 1 hit
PfamiView protein in Pfam
PF00080 Sod_Cu, 1 hit
PRINTSiPR00068 CUZNDISMTASE
SUPFAMiSSF49329 SSF49329, 1 hit
PROSITEiView protein in PROSITE
PS00087 SOD_CU_ZN_1, 1 hit
PS00332 SOD_CU_ZN_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSODC_SCHMA
AccessioniPrimary (citable) accession number: Q01137
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 10, 2018
This is version 116 of the entry and version 1 of the sequence. See 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
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