Reviewed, UniProtKB/Swiss-Prot P85978 (SODC_ASPNG)

Names and origin

Protein names

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

Gene names

Name:

sodC

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	154 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 By similarity. UniProtKB P00442
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2. Ref.1
Cofactor	Binds 1 copper ion per subunit By similarity. UniProtKB P00442 Binds 1 zinc ion per subunit By similarity. UniProtKB P00442
Subunit structure	Homodimer. Ref.1
Subcellular location	Cytoplasm By similarity. UniProtKB P00442
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.
Biophysicochemical properties	pH dependence: Retains over 90% of its activity between pH 5.6 and 7.0. Retains 85% of its activity at pH 4.0 and 60% of its activity at pH 12.0. Ref.1 Temperature dependence: Full activity is retained between 25 and 45 degrees Celsius.
Mass spectrometry	Molecular mass is 15821 Da from positions 2 - 154. Determined by MALDI. Ref.1 Molecular mass is 15824 Da from positions 2 - 154. Determined by ESI. Ref.1

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn] Ref.1		PRO_0000355101
Sites
	Metal binding	47	1	Copper; catalytic By similarity UniProtKB P00442
	Metal binding	49	1	Copper; catalytic By similarity UniProtKB P00442
	Metal binding	64	1	Copper; catalytic By similarity UniProtKB P00442
	Metal binding	64	1	Zinc; structural By similarity
	Metal binding	72	1	Zinc; structural By similarity UniProtKB P00442
	Metal binding	81	1	Zinc; structural By similarity UniProtKB P00442
	Metal binding	84	1	Zinc; structural By similarity UniProtKB P00442
	Metal binding	121	1	Copper; catalytic By similarity UniProtKB P00442
Amino acid modifications
	Disulfide bond	58 ↔ 147		By similarity UniProtKB P00442

Sequences

	Sequence		Length	Mass (Da)
	P85978-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 36967A7C19FB44D5	FASTA	154	15,976
	10 20 30 40 50 60 MVKAVAVIRG DSKVSGTVTF EQANENTPTT ISWNITGHDA NAERGFHVHQ FGDNTNGCTS 70 80 90 100 110 120 AGPHFNPYGK THGAPEDDER HVGDLGNFKT DAEGNAVGSK QDKLVKLIGA ESVLGRTLVV 130 140 150 HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIAA

References

[1]

"Biochemical properties of Cu/Zn-superoxide dismutase from fungal strain Aspergillus niger 26." Dolashki A., Abrashev R., Stevanovic S., Stefanova L., Ali S.A., Velkova L., Hristova R., Angelova M., Voelter W., Devreese B., Van Beeumen J., Dolashka-Angelova P. Spectrochim. Acta A Mol. Biomol. Spectrosc. 71:975-983(2008) [PubMed: 18395490] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-154, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY. Strain: 26.

Cross-references

3D structure databases
ModBase	Search...
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.
ProDom	PD000469. SOD_CU_ZN. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC_ASPNG

Accession

Primary (citable) accession number: P85978

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 4 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)