P07505 (SODCP_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

SODCP

Organism

Spinacia oleracea (Spinach)

Taxonomic identifier

3562 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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	Homotetramer.
Subcellular location	Plastid › chloroplast.
Miscellaneous	Chemical modification of Arg-211 reduces activity by 80-90%.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 68

68

Chloroplast Ref.2

Chain

69 – 222

154

Superoxide dismutase [Cu-Zn], chloroplastic

PRO_0000032852

Sites

Metal binding

114

1

Copper; catalytic

Metal binding

116

1

Copper; catalytic

Metal binding

131

1

Copper; catalytic

Metal binding

131

1

Zinc; structural

Metal binding

139

1

Zinc; structural

Metal binding

148

1

Zinc; structural

Metal binding

151

1

Zinc; structural

Metal binding

188

1

Copper; catalytic Ref.4

Amino acid modifications

Disulfide bond

125 ↔ 214

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

70 – 76

7

Beta strand

80 – 82

3

Beta strand

86 – 92

7

Beta strand

97 – 105

9

Beta strand

108 – 110

3

Beta strand

113 – 117

5

Helix

124 – 128

5

Beta strand

149 – 151

3

Beta strand

161 – 171

11

Beta strand

174 – 176

3

Beta strand

184 – 190

7

Beta strand

199 – 201

3

Turn

202 – 205

4

Beta strand

211 – 216

6

Beta strand

218 – 220

3

Sequences

	Sequence		Length	Mass (Da)
	P07505 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: 900E4061653575C1	FASTA	222	22,567
	10 20 30 40 50 60 MAAHTILASA PSHTTFSLIS PFSSTPTNAL SSSLQSSSFN GLSFKLSPTT QSLSLSTSAA 70 80 90 100 110 120 SKPLTIVAAT KKAVAVLKGT SNVEGVVTLT QEDDGPTTVN VRISGLAPGK HGFHLHEFGD 130 140 150 160 170 180 TTNGCMSTGP HFNPDKKTHG APEDEVRHAG DLGNIVANTD GVAEATIVDN QIPLTGPNSV 190 200 210 220 VGRALVVHEL EDDLGKGGHE LSPTTGNAGG RLACGVVGLT PV

References

[1]	"cDNA cloning and expression of the plastidic copper/zinc-superoxide dismutase from spinach (Spinacia oleracea L.) leaves." Sakamoto A., Ohsuga H., Wakaura M., Mitsukawa N., Hibino T., Masumura T., Sasaki Y., Tanaka K. Plant Cell Physiol. 34:965-968(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.
[2]	"Amino acid sequence of copper,zinc-superoxide dismutase from spinach leaves." Kitagawa Y., Tsunasawa S., Tanaka N., Katsube Y., Sakiyama F., Asada K. J. Biochem. 99:1289-1298(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 69-222.
[3]	"Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase." Malinowski D.P., Friedovich I. Biochemistry 18:5909-5917(1979) [PubMed] [Europe PMC] [Abstract] Cited for: INHIBITION BY CHEMICAL MODIFICATION.
[4]	"Three-dimensional structure of Cu,Zn-superoxide dismutase from spinach at 2.0-A resolution." Kitagawa Y., Tanaka N., Hata Y., Kusunoki M., Lee G.-P., Katsube Y., Asada K., Aibara S., Morita Y. J. Biochem. 109:477-485(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D10244 mRNA. Translation: BAA01088.1.

PIR

DSSPCZ. JQ0940.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SRD	X-ray	2.00	A/B/C/D	69-222	[»]

ProteinModelPortal

P07505.

SMR

P07505. Positions 69-222.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.200. 1 hit.

InterPro

IPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]

PANTHER

PTHR10003. PTHR10003. 1 hit.

Pfam

PF00080. Sod_Cu. 1 hit.
[Graphical view]

PRINTS

PR00068. CUZNDISMTASE.

SUPFAM

SSF49329. SOD_Cu_Zn. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P07505.

Entry information

Entry name

SODCP_SPIOL

Accession

Primary (citable) accession number: P07505

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1991
Last modified:	April 3, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program