Superoxide dismutase [Cu-Zn] precursor - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0AGD1 (SODC_ECOLI)

Last modified November 24, 2009. Version 41. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	b1646, JW1638

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H⁺ = O₂ + H₂O₂.
Cofactor	Binds 1 copper ion per subunit. Binds 1 zinc ion per subunit.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.
Biophysicochemical properties	Temperature dependence: Highly thermostable.

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Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.1

Chain

20 – 173

154

Superoxide dismutase [Cu-Zn]

PRO_0000032824

Sites

Metal binding

Copper; catalytic

Metal binding

Copper; catalytic

Metal binding

Copper; catalytic

Metal binding

Zinc; structural

Metal binding

101

Zinc; structural

Metal binding

109

Zinc; structural

Metal binding

112

Zinc; structural

Metal binding

147

Copper; catalytic

Amino acid modifications

Disulfide bond

74 ↔ 169

Ref.8

Secondary structure

173

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0AGD1-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 9A0CB65F03AAB197
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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

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli." Imlay K.R.C., Imlay J.A. J. Bacteriol. 178:2564-2571(1996) [PubMed: 8626323] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-36. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins." Battistoni A., Folcarelli S., Gabbianelli R., Capo C., Rotilio G. Biochem. J. 320:713-716(1996) [PubMed: 9003353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-173. Strain: QC871.
[5]	"Escherichia coli expresses a copper- and zinc-containing superoxide dismutase." Benov L.T., Fridovich I. J. Biol. Chem. 269:25310-25314(1994) [PubMed: 7929223] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization." Benov L.T., Chang L.Y., Day B., Fridovich I. Arch. Biochem. Biophys. 319:508-511(1995) [PubMed: 7786035] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli." Battistoni A., Rotilio G. FEBS Lett. 374:199-202(1995) [PubMed: 7589534] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography." Pesce A., Capasso C., Battistoni A., Folcarelli S., Rotilio G., Desideri A., Bolognesi M. J. Mol. Biol. 274:408-420(1997) [PubMed: 9405149] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-173, DISULFIDE BOND.

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Cross-references

Sequence databases

U51242 Genomic DNA. Translation: AAB03729.1.
U00096 Genomic DNA. Translation: AAC74718.1.
AP009048 Genomic DNA. Translation: BAE76489.1.
X97766 Genomic DNA. Translation: CAA66363.1.

PIR

JC6004.

RefSeq

AP_002268.1.
NP_416163.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ESO	X-ray	2.00	A	20-173	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0AGD1.

Genome annotation databases

GeneID

945343.

GenomeReviews

Gene locus JW1638 in contig AP009048_GR.
Gene locus b1646 in contig U00096_GR.

KEGG

ecj:JW1638.
eco:b1646.

Organism-specific databases

EchoBASE

EB3195.

EcoGene

EG13419. sodC.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AGD1.

OMA

HGFHLHA

Enzyme and pathway databases

BioCyc

EcoCyc:G6886-MON.
ECOL168927:B1646-MON.
MetaCyc:G6886-MON.

Gene expression databases

Genevestigator

P0AGD1.

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]

PROSITE

PS00087. SOD_CU_ZN_1. False negative.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

SODC_ECOLI

Accession

Primary (citable) accession number: P0AGD1
Secondary accession number(s): P53635, P96756, Q2MB67

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	November 24, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families