Reviewed, UniProtKB/Swiss-Prot Q55GQ5 (SODC1_DICDI)

Names and origin

Protein names

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

Gene names

Name:	sodA
ORF Names:	DDB_G0267420

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	153 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Developmental stage	Expressed in cells in the growth phase and throughout the developmental phases. Ref.3
Induction	By H2O2 exposure but not by UV irradiation. Ref.3
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
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
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
	Chain	1 – 153	153	Superoxide dismutase [Cu-Zn] 1		PRO_0000311820
Sites
	Metal binding	46	1	Copper; catalytic By similarity
	Metal binding	48	1	Copper; catalytic By similarity
	Metal binding	63	1	Copper; catalytic By similarity
	Metal binding	63	1	Zinc; structural By similarity
	Metal binding	71	1	Zinc; structural By similarity
	Metal binding	80	1	Zinc; structural By similarity
	Metal binding	83	1	Zinc; structural By similarity
	Metal binding	120	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 146		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55GQ5-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 8DA20D942E832098	FASTA	153	15,856
	10 20 30 40 50 60 MSKTAVCVIK GEKVNGVVKF TQENKDSPVT VNYDITGLEK GEHGFHVHAF GDTTNGCVSA 70 80 90 100 110 120 GPHFNPFGKN HGAPSDEDRH VGDLGNIVAD GESNTKGTIS DKIISLFGEH TIVGRTMVVH 130 140 150 ADQDDLGKGG KPDSLTTGAA GARLGCGVIG VSQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Differential developmental expression and cell type specificity of Dictyostelium catalases and their response to oxidative stress and UV-light." Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S., Alexander H. Biochim. Biophys. Acta 1492:295-310(2000) [PubMed: 11004503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-153. Strain: AX3-1.
[3]	"Copper/zinc superoxide dismutases in Dictyostelium discoideum: amino acid sequences and expression kinetics." Tsuji A., Akaza Y., Kodaira K., Yasukawa H. J. Biochem. Mol. Biol. Biophys. 6:215-220(2002) [PubMed: 12186757] [Abstract] Cited for: DEVELOPMENTAL STAGE, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000003 Genomic DNA. Translation: EAL73162.1. AF092899 mRNA. Translation: AAC62106.1.
RefSeq	XP_647129.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3398817.
GenomeReviews	Gene locus sodA in contig CM000150_GR.
KEGG	ddi:DDB_0191290.
Organism-specific databases
dictyBase	DDB_G0267420. sodA.
Phylogenomic databases
OMA	HAGQDDL.
Enzyme and pathway databases
BRENDA	1.15.1.1. 424.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC1_DICDI

Accession

Primary (citable) accession number: Q55GQ5
Secondary accession number(s): O77243

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)