Superoxide dismutase [Cu-Zn] (P0AGD1)

Identification
Name:Superoxide dismutase [Cu-Zn]
Synonyms:
  • Bacteriocuprein
Gene Name:sodC
Enzyme Class:
Biological Properties
General Function:Involved in superoxide metabolic process
Specific Function:Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:Not Available
KEGG Reactions:
2.0Thumb+2.0Thumb ↔ 1.0Thumb+1.0Thumb
2.0Hydrogen ion + 2.0superoxide ↔ 1.0Oxygen + 1.0Hydrogen peroxide
ReactionCard
EcoCyc Reactions:
2.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb
2.0Hydrogen ion + 2.0Superoxide anion → 1.0Hydrogen peroxide + 1.0Oxygen
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.0Superoxide anion → 1.0Hydrogen peroxide + 1.0Oxygen
ReactionCard
Complex Reactions:
2.0Thumb+2.0Thumb → 1.0Thumb+1.0Thumb
2.0superoxide + 2.0Hydrogen ion → 1.0Oxygen + 1.0Hydrogen peroxide
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB23001superoxideMetaboCard
ECMDB21285Superoxide anionMetaboCard
GO Classification:
Function
binding
cation binding
ion binding
metal ion binding
Process
cellular metabolic process
metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
Gene Properties
Blattner:b1646
Gene OrientationCounterclockwise
Centisome Percentage:37.12
Left Sequence End1722158
Right Sequence End1722679
Gene Sequence:
>522 bp
ATGCAACTGAACAAAGTGCTGAAAGGGCTGATGATTGCTCTGCCTGTTATGGCAATTGCG
GCATGTTCTTCCAACAAGAACGCCAGCAATGACGGCAGCGAAGGCATGCTGGGTGCCGGC
ACTGGTATGGATGCGAACGGCGGCAACGGCAACATGTCTTCCGAAGAGCAGGCTCGTCTG
CAAATGCAACAGCTGCAGCAGAACAACATCGTTTACTTCGATCTGGACAAGTACGATATC
CGTTCTGACTTCGCTCAAATGCTGGATGCACATGCAAACTTCCTGCGTAGCAACCCGTCT
TACAAAGTCACCGTAGAAGGTCACGCGGACGAACGTGGTACTCCGGAATACAACATCTCC
CTGGGTGAACGTCGTGCGAACGCCGTTAAGATGTACCTGCAGGGTAAAGGCGTTTCTGCA
GACCAGATCTCCATCGTTTCTTACGGTAAAGAAAAACCTGCAGTACTGGGTCATGACGAA
GCGGCATACTCCAAAAACCGTCGTGCGGTACTGGTTTACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:173
Protein Molecular Weight:17681
Protein Theoretical pI:6
PDB File:1ESO
Signaling Regions:
  • 1-19
Transmembrane Regions:
  • None
Protein Sequence:
>Superoxide dismutase [Cu-Zn]
MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALP
PGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNN
DGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK
References
External Links:
ResourceLink
Uniprot ID:P0AGD1
Uniprot Name:SODC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651333
PDB ID:1ESO
Ecogene ID:EG13419
Ecocyc:EG13419
ColiBase:b1646
Kegg Gene:b1646
EchoBASE ID:EB3195
CCDB:SODC_ECOLI
BacMap:16129604
General Reference:
  • Battistoni, A., Folcarelli, S., Gabbianelli, R., Capo, C., Rotilio, G. (1996). "The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins." Biochem J 320 ( Pt 3):713-716. Pubmed: 9003353
  • Battistoni, A., Rotilio, G. (1995). "Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli." FEBS Lett 374:199-202. Pubmed: 7589534
  • Benov, L. T., Fridovich, I. (1994). "Escherichia coli expresses a copper- and zinc-containing superoxide dismutase." J Biol Chem 269:25310-25314. Pubmed: 7929223
  • Benov, L., Chang, L. Y., Day, B., Fridovich, I. (1995). "Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization." Arch Biochem Biophys 319:508-511. Pubmed: 7786035
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Imlay, K. R., Imlay, J. A. (1996). "Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli." J Bacteriol 178:2564-2571. Pubmed: 8626323
  • Pesce, A., Capasso, C., Battistoni, A., Folcarelli, S., Rotilio, G., Desideri, A., Bolognesi, M. (1997). "Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography." J Mol Biol 274:408-420. Pubmed: 9405149