Superoxide dismutase [Fe] (P0AGD3)

Identification
Name:Superoxide dismutase [Fe]
Synonyms:Not Available
Gene Name:sodB
Enzyme Class:
Biological Properties
General Function:Involved in superoxide dismutase activity
Specific Function:Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Cellular Location:Not Available
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
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB23001superoxideMetaboCard
ECMDB21285Superoxide anionMetaboCard
GO Classification:
Function
antioxidant activity
binding
cation binding
ion binding
metal ion binding
superoxide dismutase activity
Process
cellular metabolic process
metabolic process
oxidation reduction
oxygen and reactive oxygen species metabolic process
superoxide metabolic process
Gene Properties
Blattner:b1656
Gene OrientationClockwise
Centisome Percentage:37.36
Left Sequence End1733402
Right Sequence End1733983
Gene Sequence:
>582 bp
ATGACTGACTACCTGTTACTGTTTGTCGGAACTGTACTGGTCAATAACTTTGTACTGGTC
AAGTTTCTCGGTCTCTGTCCGTTTATGGGGGTTTCCAAAAAACTGGAAACCGCGATGGGC
ATGGGGCTGGCAACAACGTTTGTGATGACGCTGGCGTCTATTTGCGCCTGGCTTATCGAT
ACGTGGATTTTGATCCCACTTAATCTGATTTACCTGCGCACCCTGGCATTTATTCTGGTG
ATTGCTGTGGTCGTGCAGTTCACCGAGATGGTGGTGCGCAAAACCAGCCCGGTGCTTTAC
CGTCTGCTGGGGATTTTTTTGCCGCTTATCACCACCAACTGTGCAGTGCTCGGCGTGGCG
TTGCTGAATATCAATCTCGGGCACAATTTCTTGCAGTCGGCGCTGTACGGTTTTTCCGCC
GCTGTCGGTTTCTCGCTGGTGATGGTGCTCTTCGCCGCCATCCGCGAACGCCTTGCTGTG
GCTGATGTCCCGGCACCTTTTCGCGGTAATGCCATTGCGTTAATTACCGCAGGTCTTATG
TCTCTGGCCTTTATGGGCTTTAGTGGTTTGGTGAAGTTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:193
Protein Molecular Weight:21266
Protein Theoretical pI:6
PDB File:1ISC
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Superoxide dismutase [Fe]
MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSS
EGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFG
SGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWA
LVNWEFVAKNLAA
References
External Links:
ResourceLink
Uniprot ID:P0AGD3
Uniprot Name:SODF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675048
PDB ID:1ISC
Ecogene ID:EG10954
Ecocyc:EG10954
ColiBase:b1656
Kegg Gene:b1656
EchoBASE ID:EB0947
CCDB:SODF_ECOLI
BacMap:16129614
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Carlioz, A., Ludwig, M. L., Stallings, W. C., Fee, J. A., Steinman, H. M., Touati, D. (1988). "Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures." J Biol Chem 263:1555-1562. Pubmed: 2447093
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Schinina, M. E., Maffey, L., Barra, D., Bossa, F., Puget, K., Michelson, A. M. (1987). "The primary structure of iron superoxide dismutase from Escherichia coli." FEBS Lett 221:87-90. Pubmed: 3305077
  • Sorkin, D. L., Miller, A. F. (1997). "Spectroscopic measurement of a long-predicted active site pK in iron-superoxide dismutase from Escherichia coli." Biochemistry 36:4916-4924. Pubmed: 9125513
  • Stallings, W. C., Powers, T. B., Pattridge, K. A., Fee, J. A., Ludwig, M. L. (1983). "Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels." Proc Natl Acad Sci U S A 80:3884-3888. Pubmed: 6346322
  • Steinman, H. M., Hill, R. L. (1973). "Sequence homologies among bacterial and mitochondrial superoxide dismutases." Proc Natl Acad Sci U S A 70:3725-3729. Pubmed: 4590170
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842