Sulfoxide reductase catalytic subunit YedY

Details

Name
Sulfoxide reductase catalytic subunit YedY
Synonyms
  • 1.8.-.-
Gene Name
yedY
Organism
Escherichia coli O157:H7
Amino acid sequence
>lcl|BSEQ0019209|Sulfoxide reductase catalytic subunit YedY
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPA
GKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEV
AKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFE
TIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLI
VPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGS
GGILDVQRQPTLLFNGYADQVASLYRGLDLRENF
Number of residues
334
Molecular Weight
37356.555
Theoretical pI
9.44
GO Classification
Functions
metal ion binding / molybdopterin cofactor binding / oxidoreductase activity, acting on a sulfur group of donors
Processes
nitrate assimilation
Components
periplasmic space
General Function
Oxidoreductase activity, acting on a sulfur group of donors
Specific Function
The exact function is not known. Can catalyze the reduction of a variety of substrates like dimethyl sulfoxide, trimethylamine N-oxide, phenylmethyl sulfoxide and L-methionine sulfoxide. Cannot reduce cyclic N-oxides. Shows no activity as sulfite oxidase.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0019210|Sulfoxide reductase catalytic subunit YedY (yedY)
ATGAAAAAGAATCAATTTTTAAAAGAATCAGATGTTACGGCCGAGTCGGTATTCTTTATG
AAGCGTCGGCAGGTGTTAAAAGCACTGGGCATCAGCGCAGCTGCACTTTCTTTGCCTCAC
GCTGCGCATGCCGATCTGCTTAGCTGGTTTAAAGGGAACGATCGCCCACCCGCCCCCGCC
GGAAAAGCGCTGGAGTTCAGCAAGCCTGCCGCCTGGCAAAATAACCTGCCACTGACGCCA
GCAGATAAAGTCTCCGGTTATAACAACTTCTATGAATTCSGGCTGGATAAAGCCGATCCC
GCCGCTAATGCTGGTAGCCTGAAAACCGATCCATGGACACTGAAAATCAGCGGCGAAGTG
GCAAAACCATTGACCCTCGATCACGATGATTTAACCCGTCGCTTCCCGCTGGAAGAGCGT
ATTTATCGTATGCGCTGCGTGGAAGCGTGGTCGATGGTGGTGCCGTGGATTGGTTTTCCG
CTGCACAAATTGCTGGCGCTTGCCGAACCCACCAGCAATGCGAAGTATGTCGCTTTCGAA
ACAATTTATGCACCGGAACAGATGCCAGGCCAGCAGGACCGCTTTATCGGCGGCGGGCTG
AAATATCCTTATGTCGAAGGATTGCGTCTCGACGAAGCAATGCATCCGCTCACACTGATG
ACCGTAGGTGTTTATGGCAAGGCGTTACCGCCACAAAATGGCGCGCCGGTGCGACTGATT
GTGCCGTGGAAATATGGCTTTAAAGGGATTAAATCGATCGTCAGTATTAAGCTGACCCGC
GAGCGTCCGCCAACCACCTGGAATCTGGCAGCGCCTGACGAATACGGTTTTTACGCCAAC
GTTAATCCGCATGTTGATCACCCACGCTGGTCACAGGCTACCGAACGATTTATTGGTTCA
GGCGGCATCCTCGATGTACAGCGCCAGCCAACGCTACTGTTTAATGGTTACGCCGACCAG
GTGGCATCGCTGTATCGTGGCCTGGATTTGCGGGAGAATTTCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ8XB74
UniProtKB Entry NameYEDY_ECO57
GenBank Protein ID12516082
GenBank Gene IDAE005174
General References
  1. Perna NT, Plunkett G 3rd, Burland V, Mau B, Glasner JD, Rose DJ, Mayhew GF, Evans PS, Gregor J, Kirkpatrick HA, Posfai G, Hackett J, Klink S, Boutin A, Shao Y, Miller L, Grotbeck EJ, Davis NW, Lim A, Dimalanta ET, Potamousis KD, Apodaca J, Anantharaman TS, Lin J, Yen G, Schwartz DC, Welch RA, Blattner FR: Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature. 2001 Jan 25;409(6819):529-33. [Article]
  2. Hayashi T, Makino K, Ohnishi M, Kurokawa K, Ishii K, Yokoyama K, Han CG, Ohtsubo E, Nakayama K, Murata T, Tanaka M, Tobe T, Iida T, Takami H, Honda T, Sasakawa C, Ogasawara N, Yasunaga T, Kuhara S, Shiba T, Hattori M, Shinagawa H: Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12. DNA Res. 2001 Feb 28;8(1):11-22. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03904Ureaapproved, investigationalunknownDetails