Peptide methionine sulfoxide reductase msrB (P0A746)

Identification
Name:Peptide methionine sulfoxide reductase msrB
Synonyms:
  • Peptide-methionine (R)-S-oxide reductase
Gene Name:msrB
Enzyme Class:
Biological Properties
General Function:Involved in peptide-methionine-(S)-S-oxide reductase activity
Specific Function:Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Peptide-L-methionine+1.0Thioredoxin disulfide+1.0Thumb ↔ 1.0Peptide-L-methionine (R)-S-oxide+1.0Thumb
1.0Peptide-L-methionine + 1.0Thioredoxin disulfide + 1.0Water ↔ 1.0Peptide-L-methionine (R)-S-oxide + 1.0Thioredoxin
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 (R)-S-oxide+1.0thioredoxin
1.0Peptide-L-methionine + 1.0thioredoxin disulfide + 1.0Water → 1.0peptide-L-methionine (R)-S-oxide + 1.0thioredoxin
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00696L-MethionineMetaboCard
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
peptide-methionine-(S)-S-oxide reductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1778
Gene OrientationCounterclockwise
Centisome Percentage:40.09
Left Sequence End1860040
Right Sequence End1860453
Gene Sequence:
>414 bp
ATGATCTGGAAACGCCATTTAACGCTCGACGAACTGAACGCCACCAGCGATAACACAATG
GTGGCGCATCTGGGAATTGTGTATACCCGTCTGGGCGATGATGTGCTGGAAGCCGAAATG
CCGGTTGATACCCGTACTCATCAGCCGTTCGGTTTACTACATGGCGGCGCGTCGGCGGCG
CTGGCGGAAACGCTGGGATCGATGGCCGGATTTATGATGACCCGCGACGGACAGTGTGTG
GTAGGCACAGAACTTAATGCAACACACCATCGCCCGGTGTCTGAGGGAAAGGTACGCGGC
GTCTGCCAGCCGCTGCATCTTGGTCGGCAAAATCAGAGCTGGGAAATCGTCGTTTTCGAT
GAACAGGGGCGGCGTTGCTGCACTTGTCGGCTGGGTACGGCAGTTTTGGGATGA
Protein Properties
Pfam Domain Function:
Protein Residues:137
Protein Molecular Weight:15451
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Peptide methionine sulfoxide reductase msrB
MANKPSAEELKKNLSEMQFYVTQNHGTEPPFTGRLLHNKRDGVYHCLICDAPLFHSQTKY
DSGCGWPSFYEPVSEESIRYIKDLSHGMQRIEIRCGNCDAHLGHVFPDGPQPTGERYCVN
SASLRFTDGENGEEING
References
External Links:
ResourceLink
Uniprot ID:P0A746
Uniprot Name:MSRB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674718
Ecogene ID:EG12394
Ecocyc:EG12394
ColiBase:b1778
Kegg Gene:b1778
EchoBASE ID:EB2295
CCDB:MSRB_ECOLI
BacMap:16129732
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
  • Borodovsky, M., Rudd, K. E., Koonin, E. V. (1994). "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Nucleic Acids Res 22:4756-4767. Pubmed: 7984428
  • Branlant, G., Branlant, C. (1985). "Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase." Eur J Biochem 150:61-66. Pubmed: 2990926
  • Grimaud, R., Ezraty, B., Mitchell, J. K., Lafitte, D., Briand, C., Derrick, P. J., Barras, F. (2001). "Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase." J Biol Chem 276:48915-48920. Pubmed: 11677230
  • 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
  • Olry, A., Boschi-Muller, S., Yu, H., Burnel, D., Branlant, G. (2005). "Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B." Protein Sci 14:2828-2837. Pubmed: 16251365