A2QMY6 (SODC_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	sodC
ORF Names:	An07g03770

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

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. UniProtKB P00442
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2. UniProtKB P00442
Cofactor	Binds 1 copper ion per subunit By similarity. UniProtKB P00442 Binds 1 zinc ion per subunit By similarity. UniProtKB P00442
Subunit structure	Homodimer By similarity. UniProtKB P00442
Subcellular location	Cytoplasm By similarity UniProtKB P00442.
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	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm 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
	Initiator methionine	1	1	Removed By similarity UniProtKB P00442
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn] UniProtKB P00442		PRO_0000355100
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)
	A2QMY6 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: C8679562F6FB52AF	FASTA	154	15,960
	10 20 30 40 50 60 MVKAVAVIRG DSKVSGTVTF EQANENTPTT ISWNITGHDA NAERGFHVHQ FGDNTNGCTS 70 80 90 100 110 120 AGPHFNPFGK THGAPEDDER HVGDLGNFKT DAEGNAVGSK QDKLVKLIGA ESVLGRTLVV 130 140 150 HAGTDDLGRG GNEESKKTGN AGPRPACGVI GIAA

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270128 Genomic DNA. Translation: CAK48127.1.
RefSeq	XP_001391459.1. XM_001391422.2.
3D structure databases
ProteinModelPortal	A2QMY6.
SMR	A2QMY6. Positions 2-152.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00005537.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00005648; CADANGAP00005537; CADANGAG00005648.
GeneID	4981643.
KEGG	ang:ANI_1_470064.
Phylogenomic databases
HOGENOM	HOG000263447.
KO	K04565.
OrthoDB	EOG4X3M9S.
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...

Entry information

Entry name

SODC_ASPNC

Accession

Primary (citable) accession number: A2QMY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program