Alkyl hydroperoxide reductase subunit C (P0AE08)

Identification
Name:Alkyl hydroperoxide reductase subunit C
Synonyms:
  • Alkyl hydroperoxide reductase protein C22
  • Peroxiredoxin
  • SCRP-23
  • Sulfate starvation-induced protein 8
  • SSI8
  • Thioredoxin peroxidase
Gene Name:ahpC
Enzyme Class:
Biological Properties
General Function:Involved in peroxiredoxin activity
Specific Function:Directly reduces organic hydroperoxides in its reduced dithiol form
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2.0Thiol-containing reductant+1.0ROOH ↔ 1.0Oxidized thiol-containing reductant+1.0Thumb+1.0ROH
2.0Thiol-containing reductant + 1.0ROOH ↔ 1.0Oxidized thiol-containing reductant + 1.0Water + 1.0ROH
ReactionCard
Complex Reactions:
2.0R'-SH+1.0ROOH → 1.0R'-S-S-R'+1.0Thumb+1.0ROH
2.0R'-SH + 1.0ROOH → 1.0R'-S-S-R' + 1.0Water + 1.0ROH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00494WaterMetaboCard
GO Classification:
Function
antioxidant activity
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
peroxiredoxin activity
Process
cell redox homeostasis
cellular homeostasis
cellular process
metabolic process
oxidation reduction
Gene Properties
Blattner:b0605
Gene OrientationClockwise
Centisome Percentage:13.75
Left Sequence End638168
Right Sequence End638731
Gene Sequence:
>564 bp
ATGTCCTTGATTAACACCAAAATTAAACCTTTTAAAAACCAGGCATTCAAAAACGGCGAA
TTCATCGAAATCACCGAAAAAGATACCGAAGGCCGCTGGAGCGTCTTCTTCTTCTACCCG
GCTGACTTTACTTTCGTATGCCCGACCGAACTGGGTGACGTTGCTGACCACTACGAAGAA
CTGCAGAAACTGGGCGTAGACGTATACGCAGTATCTACCGATACTCACTTCACCCACAAA
GCATGGCACAGCAGCTCTGAAACCATCGCTAAAATCAAATATGCGATGATCGGCGACCCG
ACTGGCGCCCTGACCCGTAACTTCGACAACATGCGTGAAGATGAAGGTCTGGCTGACCGT
GCGACCTTCGTTGTTGACCCGCAGGGTATCATCCAGGCAATCGAAGTTACCGCTGAAGGC
ATTGGCCGTGACGCGTCTGACCTGCTGCGTAAAATCAAAGCAGCACAGTACGTAGCTTCT
CACCCAGGTGAAGTTTGCCCGGCTAAATGGAAAGAAGGTGAAGCAACTCTGGCTCCGTCT
CTGGACCTGGTTGGTAAAATCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:187
Protein Molecular Weight:20761
Protein Theoretical pI:5
PDB File:1KYG
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Alkyl hydroperoxide reductase subunit C
MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEE
LQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADR
ATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPS
LDLVGKI
References
External Links:
ResourceLink
Uniprot ID:P0AE08
Uniprot Name:AHPC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062222
PDB ID:1KYG
Ecogene ID:EG11384
Ecocyc:EG11384
ColiBase:b0605
Kegg Gene:b0605
EchoBASE ID:EB1357
CCDB:AHPC_ECOLI
BacMap:16128588
General Reference:
  • 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
  • Cha, M. K., Kim, H. K., Kim, I. H. (1995). "Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli." J Biol Chem 270:28635-28641. Pubmed: 7499381
  • 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
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Quadroni, M., Staudenmann, W., Kertesz, M., James, P. (1996). "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Eur J Biochem 239:773-781. Pubmed: 8774726
  • Smillie, D. A., Hayward, R. S., Suzuki, T., Fujita, N., Ishihama, A. (1992). "Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome." J Bacteriol 174:3826-3827. Pubmed: 1592833
  • Ueshima, R., Fujita, N., Ishihama, A. (1992). "Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit." Biochem Biophys Res Commun 184:634-639. Pubmed: 1575737
  • 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