Q9RU48 (SODC_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	sodC
Ordered Locus Names:	DR_1546

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	182 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 Potential. Binds 1 zinc ion per subunit Potential.
Subcellular location	Cell membrane; Lipid-anchor Potential.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.
Caution	Lacks the last conserved histidine that binds copper.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	periplasmic space Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome 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
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 182	163	Superoxide dismutase [Cu-Zn]		PRO_0000032841
Sites
	Metal binding	69	1	Copper; catalytic By similarity
	Metal binding	71	1	Copper; catalytic By similarity
	Metal binding	95	1	Copper; catalytic By similarity
	Metal binding	95	1	Zinc; structural By similarity
	Metal binding	104	1	Zinc; structural By similarity
	Metal binding	115	1	Zinc; structural By similarity
	Metal binding	118	1	Zinc; structural By similarity
Amino acid modifications
	Lipidation	20	1	N-palmitoyl cysteine Potential
	Lipidation	20	1	S-diacylglycerol cysteine Potential
	Disulfide bond	76 ↔ 175		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RU48 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 96749572F393CA1A	FASTA	182	18,787
	10 20 30 40 50 60 MFRTLTVVPL LALGLSLSAC ADLGQPTVRA DLLDQTGKVT GTATFSPSPI GTRVSIEVSG 70 80 90 100 110 120 LKAGPHGLHI HENPNCNPGP DAQGQTIPFG AAGGHFDPGA SHNHDGPHAR NDQGHGGDLP 130 140 150 160 170 180 MITVGEDGKG RLNFDTNRLK MTGPTGVLGR SIVIHADADD YQTNPAGNSG GRERCGVFQA IN

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF11107.1.
PIR	B75383.
RefSeq	NP_295269.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RU48.
ModBase	Search...
Protein-protein interaction databases
STRING	243230.DR_1546.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF11107; AAF11107; DR_1546.
GeneID	1797544.
KEGG	dra:DR_1546.
PATRIC	21630704. VBIDeiRad64572_1748.
Phylogenomic databases
eggNOG	COG2032.
HOGENOM	HOG000263448.
KO	K04565.
OMA	APRFESS.
ProtClustDB	CLSK2460292.
Enzyme and pathway databases
BioCyc	DRAD243230:GH46-1915-MONOMER.
Family and domain databases
Gene3D	2.60.40.200. 1 hit.
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
PANTHER	PTHR10003. PTHR10003. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS51257. PROKAR_LIPOPROTEIN. 1 hit. PS00087. SOD_CU_ZN_1. False negative. PS00332. SOD_CU_ZN_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC_DEIRA

Accession

Primary (citable) accession number: Q9RU48

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program