Q54G70 (SODC5_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn] 5
EC=1.15.1.1

Gene names

Name:	sodE
ORF Names:	DDB_G0290343

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
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.
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 Reference proteome
Gene Ontology (GO)
Biological process	removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide anion generation Inferred from sequence or structural similarity. Source: dictyBase
Cellular component	cytosol Inferred from sequence or structural similarity. Source: dictyBase mitochondrial intermembrane space Inferred from sequence or structural similarity. Source: dictyBase
Molecular function	copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activity Inferred from sequence or structural similarity. Source: dictyBase zinc ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 152	152	Superoxide dismutase [Cu-Zn] 5		PRO_0000327854
Sites
	Metal binding	44	1	Copper; catalytic By similarity
	Metal binding	46	1	Copper; catalytic By similarity
	Metal binding	61	1	Copper; catalytic By similarity
	Metal binding	61	1	Zinc; structural By similarity
	Metal binding	69	1	Zinc; structural By similarity
	Metal binding	78	1	Zinc; structural By similarity
	Metal binding	81	1	Zinc; structural By similarity
	Metal binding	118	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	55 ↔ 144		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54G70 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A9FE41F3A7C08ADA	FASTA	152	16,148
	10 20 30 40 50 60 MSAICVIKGD GVDGIINFKQ NDNKSPVIIS GVISGLKEGK HGFHVHEFGD TTNGCLSAGA 70 80 90 100 110 120 HFNPFKKEHG SPNDENRHVG DLGNIESNKD KKSIINITDN IITLFGQNSI IGRSIVVHDK 130 140 150 EDDLGRGNSQ DSKITGNAGS RLGCGIIALS KI

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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000162 Genomic DNA. Translation: EAL62298.1.
RefSeq	XP_635813.1. XM_630721.1.
3D structure databases
HSSP	HSSP built from PDB template 1HL5 based on UniProtKB P00441.
ProteinModelPortal	Q54G70.
SMR	Q54G70. Positions 1-151.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0237961; DDB0237961; DDB_G0290343.
GeneID	8627619.
GenomeReviews	Gene locus sodE in contig CM000154_GR.
KEGG	ddi:DDB_G0290343.
Organism-specific databases
dictyBase	DDB_G0290343. sodE.
Phylogenomic databases
eggNOG	KOG0441.
GeneTree	EPrGT00050000005882.
HOGENOM	HBG609879.
OMA	TQEGDGP.
PhylomeDB	Q54G70.
ProtClustDB	CLSZ2429689.
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

SODC5_DICDI

Accession

Primary (citable) accession number: Q54G70

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)