Reviewed, UniProtKB/Swiss-Prot Q8X1S6 (SODC_ASPFL)

Names and origin

Protein names

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

Gene names

Name:

sodC

Organism

Aspergillus flavus

Taxonomic identifier

5059 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
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
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 By similarity
	Chain	2 – 153	152	Superoxide dismutase [Cu-Zn]		PRO_0000164107
Sites
	Metal binding	46	1	Copper By similarity
	Metal binding	48	1	Copper By similarity
	Metal binding	63	1	Copper By similarity
	Metal binding	63	1	Zinc By similarity
	Metal binding	71	1	Zinc By similarity
	Metal binding	80	1	Zinc By similarity
	Metal binding	83	1	Zinc By similarity
	Metal binding	120	1	Copper By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 146		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8X1S6-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: FC17B6425DD9C7B4	FASTA	153	15,895
	10 20 30 40 50 60 MVKAVAVRGD SKISGTVTFE QADANAPTTV SWNITGHDAN AERAFHVHQF GDNTNGCTSA 70 80 90 100 110 120 GPHFNPFGKE HGAPEDENRH VGDLGNFKTD AEGNAVGSKQ DKLIKLIGAE SVLGRTLVIH 130 140 150 AGTDDLGRSE HPESKKTGNA GARPACGVIG IAA

References

[1]

"Homogeneity in 3-dimensional structure of Cu,Zn superoxide dismutases of Aspergillus fumigatus, Aspergillus flavus and Aspergillus nidulans." Holdom M.D., Hobby P., Lechenne B., Zaugg C., Sutton B., Monod M., Hamilton A.J. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF281059 Genomic DNA. Translation: AAL38993.1.
3D structure databases
HSSP	HSSP built from PDB template 1OZU based on UniProtKB P00441.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.15.1.1. 2238.
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_ASPFL

Accession

Primary (citable) accession number: Q8X1S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 38 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)