P0AGD2 (SODC_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Bacteriocuprein

Gene names

Name:	sodC
Ordered Locus Names:	Z2661, ECs2355

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	173 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 By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Periplasm By similarity.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
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	periplasmic space 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
	Signal peptide	1 – 19	19	By similarity
	Chain	20 – 173	154	Superoxide dismutase [Cu-Zn]		PRO_0000045306
Sites
	Metal binding	67	1	Copper; catalytic By similarity
	Metal binding	69	1	Copper; catalytic By similarity
	Metal binding	92	1	Copper; catalytic By similarity
	Metal binding	92	1	Zinc; structural By similarity
	Metal binding	101	1	Zinc; structural By similarity
	Metal binding	109	1	Zinc; structural By similarity
	Metal binding	112	1	Zinc; structural By similarity
	Metal binding	147	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	74 ↔ 169		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0AGD2 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 9A0CB65F03AAB197	FASTA	173	17,681
	10 20 30 40 50 60 MKRFSLAILA LVVATGAQAA SEKVEMNLVT SQGVGQSIGS VTITETDKGL EFSPDLKALP 70 80 90 100 110 120 PGEHGFHIHA KGSCQPATKD GKASAAESAG GHLDPQNTGK HEGPEGAGHL GDLPALVVNN 130 140 150 160 170 DGKATDAVIA PRLKSLDEIK DKALMVHVGG DNMSDQPKPL GGGGERYACG VIK

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56635.1. BA000007 Genomic DNA. Translation: BAB35778.1.
PIR	C90923. G85771.
RefSeq	NP_288082.1. NC_002655.2. NP_310382.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AGD2.
SMR	P0AGD2. Positions 20-173.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025561; EBESCP00000024454; EBESCG00000024614. EBESCT00000055213; EBESCP00000053041; EBESCG00000054261.
GeneID	914926. 961605.
GenomeReviews	Gene locus Z2661 in contig AE005174_GR. Gene locus ECs2355 in contig BA000007_GR.
KEGG	ece:Z2661. ecs:ECs2355.
PATRIC	18354038. VBIEscCol44059_2232.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010661.
HOGENOM	HBG609879.
OMA	NTNSHQG.
ProtClustDB	PRK10290.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2355-MONOMER.
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]
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS00087. SOD_CU_ZN_1. False negative. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SODC_ECO57

Accession

Primary (citable) accession number: P0AGD2
Secondary accession number(s): P53635, P96756

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program