Reviewed, UniProtKB/Swiss-Prot Q877B5 (SODC_ASPOR)

Names and origin

Protein names

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

Gene names

Name:	sodC
ORF Names:	AO090020000521

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [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	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
Technical term	Complete proteome
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 – 154	153	Superoxide dismutase [Cu-Zn]		PRO_0000164110
Sites
	Metal binding	47	1	Copper By similarity
	Metal binding	49	1	Copper By similarity
	Metal binding	64	1	Copper By similarity
	Metal binding	64	1	Zinc By similarity
	Metal binding	72	1	Zinc By similarity
	Metal binding	81	1	Zinc By similarity
	Metal binding	84	1	Zinc By similarity
	Metal binding	121	1	Copper By similarity
Amino acid modifications
	Disulfide bond	58 ↔ 147		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q877B5-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 998DB6C6CCA29F8D	FASTA	154	16,009
	10 20 30 40 50 60 MVKAVAVLRG DSKISGTVTF EQADANAPTT VSWNITGHDA NAERAFHVHQ FGDNTNGCTS 70 80 90 100 110 120 AGPHFNPFGK EHGAPEDENR HVGDLGNFKT DAEGNAVGSK QDKLIKLIGA ESVLGRTLVI 130 140 150 HAGTDDLGRS EHPESKKTGN AGARPACGVI GIAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cu,Zn superoxide dismutase-encoding gene of Aspergillus oryzae." Ishida H., Hata Y., Kawato A., Suginami K., Abe Y. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB078725 Genomic DNA. Translation: BAC56176.1. AP007167 Genomic DNA. Translation: BAE63690.1.
RefSeq	XP_001824823.1.
3D structure databases
HSSP	HSSP built from PDB template 1OZU based on UniProtKB P00441.
ModBase	Search...
Genome annotation databases
GeneID	5996909.
GenomeReviews	Gene locus sodC in contig AP007167_GR.
KEGG	aor:AO090020000521.
Enzyme and pathway databases
BRENDA	1.15.1.1. 2240.
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_ASPOR

Accession

Primary (citable) accession number: Q877B5
Secondary accession number(s): Q2U425

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 37 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)