O42724 (SODC1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn] 1
EC=1.15.1.1

Gene names

Name:	SOD1
Ordered Locus Names:	DEHA2G17732g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

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.
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.
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 Direct protein sequencing
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
	Chain	2 – 154	153	Superoxide dismutase [Cu-Zn] 1		PRO_0000164118
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
Experimental info
	Sequence conflict	2 – 3	2	AK → VQ in AAC50010. Ref.1
	Sequence conflict	145	1	P → L in AAC50010. Ref.1
	Sequence conflict	153 – 154	2	SE → TN in AAC50010. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O42724 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 673083B0716C698E	FASTA	154	15,888
	10 20 30 40 50 60 MAKAVAVLRG DSKVSGVVNF EQSSESDPTT ITWEISGNDA NALRGFHVHT FGDNTNGCTS 70 80 90 100 110 120 AGPHFNPFTK EHGAPEDDNR HVGDLGNVTT DTSGVAKGSK QDLFVKLIGQ NSILGRTVVI 130 140 150 HAGTDDLGKG GNAESKKTGN AGARPACGVI GLSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding a copper-zinc superoxide dismutase enzyme from the marine yeast Debaryomyces hansenii." Hernandez-Saavedra N.Y., Egly J.-M., Ochoa J.L. Yeast 14:573-581(1998) [PubMed: 9605507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-29. Strain: CIBNOR C-11.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF016383 mRNA. Translation: AAC50010.1. CR382139 Genomic DNA. Translation: CAG90816.1.
RefSeq	XP_462310.1. XM_462310.1.
3D structure databases
ProteinModelPortal	O42724.
SMR	O42724. Positions 3-153.
ModBase	Search...
Protein-protein interaction databases
STRING	O42724.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2905248.
GenomeReviews	Gene locus DEHA2G17732g in contig CR382139_GR.
KEGG	dha:DEHA2G17732g.
Phylogenomic databases
eggNOG	fuNOG09621.
HOGENOM	HBG609879.
OMA	IHFEQKA.
OrthoDB	EOG4X3M9S.
Family and domain databases
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
KO	K04565.
PANTHER	PTHR10003. SOD_Cu_Zn. 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

SODC1_DEBHA

Accession

Primary (citable) accession number: O42724
Secondary accession number(s): Q6BHL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 89 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program