Sulfoxide reductase catalytic subunit YedY

NameSulfoxide reductase catalytic subunit YedY
Synonyms
  • 1.8.-.-
Gene NameyedY
OrganismEscherichia coli O157:H7
Amino acid sequence
>lcl|BSEQ0019209|Sulfoxide reductase catalytic subunit YedY
MKKNQFLKESDVTAESVFFMKRRQVLKALGISAAALSLPHAAHADLLSWFKGNDRPPAPA
GKALEFSKPAAWQNNLPLTPADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEV
AKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFE
TIYAPEQMPGQQDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLI
VPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGS
GGILDVQRQPTLLFNGYADQVASLYRGLDLRENF
Number of residues334
Molecular Weight37356.555
Theoretical pI9.44
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 FunctionOxidoreductase activity, acting on a sulfur group of donors
Specific FunctionThe 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 RegionsNot Available
GenBank Protein ID12516082
UniProtKB IDQ8XB74
UniProtKB Entry NameYEDY_ECO57
Cellular LocationPeriplasm
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
GenBank Gene IDAE005174
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
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. 11206551
  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. 11258796