Peptide methionine sulfoxide reductase msrA (P0A744)

Identification
Name:Peptide methionine sulfoxide reductase msrA
Synonyms:
  • Protein-methionine-S-oxide reductase
  • Peptide-methionine (S)-S-oxide reductase
  • Peptide Met(O) reductase
Gene Name:msrA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Specific Function:Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Peptide-L-methionine+1.0Thioredoxin disulfide+1.0Thumb+1.0Thumb ↔ 1.0Peptide-L-methionine (S)-S-oxide+1.0Thumb+1.0Thumb
1.0Peptide-L-methionine + 1.0Thioredoxin disulfide + 1.0Water + 1.0L-Methionine ↔ 1.0Peptide-L-methionine (S)-S-oxide + 1.0Thioredoxin + 1.0L-methionine (S)-S-oxide
ReactionCard
Complex Reactions:
1.0Thumb+1.0Reduced Thioredoxin → 1.0Thumb+1.0Thumb+1.0Oxidized Thioredoxin
1.0Methionine sulfoxide + 1.0Reduced Thioredoxin → 1.0Water + 1.0L-Methionine + 1.0Oxidized Thioredoxin
ReactionCard
1.0Peptide-L-methionine+1.0thioredoxin disulfide+1.0Thumb → 1.0peptide-L-methionine (S)-S-oxide+1.0thioredoxin
1.0Peptide-L-methionine + 1.0thioredoxin disulfide + 1.0Water → 1.0peptide-L-methionine (S)-S-oxide + 1.0thioredoxin
ReactionCard
1.0Thumb+1.0thioredoxin disulfide+1.0Thumb → 1.0Thumb+1.0thioredoxin
1.0L-Methionine + 1.0thioredoxin disulfide + 1.0Water → 1.0L-methionine (S)-S-oxide + 1.0thioredoxin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00696L-MethionineMetaboCard
ECMDB23117L-methionine (S)-S-oxideMetaboCard
ECMDB20295L-Methionine-(S)-S-oxideMetaboCard
ECMDB02005Methionine sulfoxideMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
Process
macromolecule metabolic process
metabolic process
oxidation reduction
protein metabolic process
Gene Properties
Blattner:b4219
Gene OrientationCounterclockwise
Centisome Percentage:95.69
Left Sequence End4439561
Right Sequence End4440199
Gene Sequence:
>639 bp
ATGACGCAAGGCGCAGTGAAAACAACGGGTAAACGTTCGCGCGCAGTAAGCGCGAAGAAA
AAAGCGATTCTTAGCGCAGCACTGGACACTTTTTCACAATTCGGTTTTCACGGCACAAGG
CTGGAGCAGATCGCAGAGTTGGCGGGTGTTTCAAAAACCAATCTGCTGTATTACTTTCCG
TCAAAAGAGGCGCTGTATATTGCCGTGCTGCGGCAGATTCTCGATATCTGGCTGGCACCG
TTAAAAGCGTTTCGTGAAGATTTCGCCCCGCTGGCGGCGATCAAAGAGTACATCCGTCTG
AAGCTGGAAGTCTCACGCGATTATCCGCAGGCTTCGCGCCTGTTCTGTATGGAGATGCTG
GCAGGCGCGCCGCTGTTAATGGATGAACTGACGGGCGATTTGAAGGCATTAATTGATGAG
AAATCGGCGCTGATTGCCGGTTGGGTCAAAAGCGGCAAACTCGCGCCGATTGATCCGCAG
CATTTGATTTTTATGATTTGGGCTTCCACTCAACATTACGCCGATTTCGCCCCTCAGGTG
GAGGCGGTGACAGGCGCGACGTTGCGCGATGAGGTATTTTTCAATCAAACGGTTGAAAAC
GTGCAGCGGATTATTATTGAGGGGATTCGACCACGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:212
Protein Molecular Weight:23315
Protein Theoretical pI:5
PDB File:1FF3
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Peptide methionine sulfoxide reductase msrA
MSLFDKKHLVSPADALPGRNTPMPVATLHAVNGHSMTNVPDGMEIAIFAMGCFWGVERLF
WQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHD
PAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPF
YYAEDDHQQYLHKNPYGYCGIGGIGVCLPPEA
References
External Links:
ResourceLink
Uniprot ID:P0A744
Uniprot Name:MSRA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062576
PDB ID:1FF3
Ecogene ID:EG11433
Ecocyc:EG11433
ColiBase:b4219
Kegg Gene:b4219
EchoBASE ID:EB1403
CCDB:MSRA_ECOLI
BacMap:16132041
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
  • Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., Branlant, G. (2000). "A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli." J Biol Chem 275:35908-35913. Pubmed: 10964927
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Rahman, M. A., Nelson, H., Weissbach, H., Brot, N. (1992). "Cloning, sequencing, and expression of the Escherichia coli peptide methionine sulfoxide reductase gene." J Biol Chem 267:15549-15551. Pubmed: 1386361
  • Tete-Favier, F., Cobessi, D., Boschi-Muller, S., Azza, S., Branlant, G., Aubry, A. (2000). "Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution." Structure 8:1167-1178. Pubmed: 11080639