Reviewed, UniProtKB/Swiss-Prot Q01137 (SODC_SCHMA)

Names and origin

Protein names

Recommended name:
    Superoxide dismutase [Cu-Zn]
    EC=1.15.1.1

Gene names

Name:

SOD

Organism

Schistosoma mansoni (Blood fluke)

Taxonomic identifier

6183 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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. Ref.4
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	antioxidant 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 153

153

Superoxide dismutase [Cu-Zn]

PRO_0000164105

Sites

Metal binding

45

1

Copper; catalytic

Metal binding

47

1

Copper; catalytic

Metal binding

62

1

Copper; catalytic

Metal binding

62

1

Zinc; structural

Metal binding

70

1

Zinc; structural

Metal binding

79

1

Zinc; structural

Metal binding

82

1

Zinc; structural

Metal binding

119

1

Copper; catalytic

Amino acid modifications

Disulfide bond

56 ↔ 145

Experimental info

Sequence conflict

115

1

T → S in AAA29935. Ref.2

Sequence conflict

148

1

I → V Ref.2

Sequence conflict

148

1

I → V Ref.3

Secondary structure

1

.

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153

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

10 – 12

3

Beta strand

14 – 23

10

Beta strand

28 – 36

9

Beta strand

39 – 48

10

Turn

53 – 56

4

Helix

57 – 59

3

Beta strand

82 – 88

7

Beta strand

94 – 102

9

Beta strand

104 – 106

3

Helix

107 – 109

3

Beta strand

114 – 121

8

Helix

133 – 136

4

Beta strand

141 – 147

7

Sequences

	Sequence		Length	Mass (Da)
	Q01137-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D30014FDBD34593A	FASTA	153	15,721
	10 20 30 40 50 60 MKAVCVMTGT AGVKGVVKFT QETDNGPVHV HAEFSGLKAG KHGFHVHEFG DTTNGCTSAG 70 80 90 100 110 120 AHFNPTKQEH GAPEDSIRHV GDLGNVVAGA DGNAVYNATD KLISLNGSHS IIGRTMVIHE 130 140 150 NEDDLGRGGH ELSKVTGNAG GRLACGVIGL AAE

References

[1]	"Molecular cloning of a 16-kilodalton Cu/Zn superoxide dismutase from Schistosoma mansoni." da Silva A., Lepresle T., Capron A., Pierce R.J. Mol. Biochem. Parasitol. 52:275-278(1992) [PubMed: 1620165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Schistosoma mansoni: cloning of a complementary DNA encoding a cytosolic Cu/Zn superoxide dismutase and high-yield expression of the enzymatically active gene product in Escherichia coli." Hong Z., Loverde P.T., Hammarskjold M.L., Rekosh D. Exp. Parasitol. 75:308-322(1992) [PubMed: 1426133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Schistosoma mansoni: cloning and characterization of a gene encoding cytosolic Cu/Zn superoxide dismutase." Mei H., Hirai H., Tanaka M., Hong Z., Rekosh D., Loverde P.T. Exp. Parasitol. 80:250-259(1995) [PubMed: 7895835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NMRI.
[4]	"Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni." Cardoso R.M.F., Silva C.H.T.P., Ulian de Araujo A.P., Tanaka T., Tanaka M., Garratt R.C. Acta Crystallogr. D 60:1569-1578(2004) [PubMed: 15333927] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC AND COPPER IONS, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M86867 mRNA. Translation: AAA29936.1.
M97298 mRNA. Translation: AAA29935.1.
L12159, L12008, L12158 Genomic DNA. Translation: AAC14467.1.

PIR

A49241.

RefSeq

XP_002580684.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TO4	X-ray	1.55	A/B/C/D	1-153	[»]
1TO5	X-ray	2.20	A/B/C/D	1-153	[»]

ModBase

Search...

Genome annotation databases

GeneID

8341913.

KEGG

smm:Smp_176200.2.

Organism-specific databases

CTD

8341913.

Enzyme and pathway databases

BRENDA

1.15.1.1. 1460.

Family and domain databases

InterPro

IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn.
[Graphical view]

Gene3D

G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.

PANTHER

PTHR10003. SOD_Cu_Zn. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

PROSITE

PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SODC_SCHMA

Accession

Primary (citable) accession number: Q01137

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	February 9, 2010
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)