Lactaldehyde reductase

Details

Name
Lactaldehyde reductase
Synonyms
  • 1.1.1.77
  • Propanediol oxidoreductase
Gene Name
fucO
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0037155|Lactaldehyde reductase
MANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGLA
WAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVRS
LEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDADM
MDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAGE
EMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKYR
DIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDDV
CTGGNPREATLEDIVELYHTAW
Number of residues
382
Molecular Weight
40513.025
Theoretical pI
4.91
GO Classification
Functions
ferrous iron binding / lactaldehyde reductase activity
Processes
glycol catabolic process / L-fucose catabolic process / propanediol metabolic process / rhamnose catabolic process
Components
cytosol
General Function
Lactaldehyde reductase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016660|Lactaldehyde reductase (fucO)
ATGATGGCTAACAGAATGATTCTGAACGAAACGGCATGGTTTGGTCGGGGTGCTGTTGGG
GCTTTAACCGATGAGGTGAAACGCCGTGGTTATCAGAAGGCGCTGATCGTCACCGATAAA
ACGCTGGTGCAATGCGGCGTGGTGGCGAAAGTGACCGATAAGATGGATGCTGCAGGGCTG
GCATGGGCGATTTACGACGGCGTAGTGCCCAACCCAACAATTACTGTCGTCAAAGAAGGG
CTCGGTGTATTCCAGAATAGCGGCGCGGATTACCTGATCGCTATTGGTGGTGGTTCTCCA
CAGGATACTTGTAAAGCGATTGGCATTATCAGCAACAACCCGGAGTTTGCCGATGTGCGT
AGCCTGGAAGGGCTTTCCCCGACCAATAAACCCAGTGTACCGATTCTGGCAATTCCTACC
ACAGCAGGTACTGCGGCAGAAGTGACCATTAACTACGTGATCACTGACGAAGAGAAACGG
CGCAAGTTTGTTTGCGTTGATCCGCATGATATCCCGCAGGTGGCGTTTATTGACGCTGAC
ATGATGGATGGTATGCCTCCAGCGCTGAAAGCTGCGACGGGTGTCGATGCGCTCACTCAT
GCTATTGAGGGGTATATTACCCGTGGCGCGTGGGCGCTAACCGATGCACTGCACATTAAA
GCGATTGAAATCATTGCTGGGGCGCTGCGAGGATCGGTTGCTGGTGATAAGGATGCCGGA
GAAGAAATGGCGCTCGGGCAGTATGTTGCGGGTATGGGCTTCTCGAATGTTGGGTTAGGG
TTGGTGCATGGTATGGCGCATCCACTGGGCGCGTTTTATAACACTCCACACGGTGTTGCG
AACGCCATCCTGTTACCGCATGTCATGCGTTATAACGCTGACTTTACCGGTGAGAAGTAC
CGCGATATCGCGCGCGTTATGGGCGTGAAAGTGGAAGGTATGAGCCTGGAAGAGGCGCGT
AATGCCGCTGTTGAAGCGGTGTTTGCTCTCAACCGTGATGTCGGTATTCCGCCACATTTG
CGTGATGTTGGTGTACGCAAGGAAGACATTCCGGCACTGGCGCAGGCGGCACTGGATGAT
GTTTGTACCGGTGGCAACCCGCGTGAAGCAACGCTTGAGGATATTGTAGAGCTTTACCAT
ACCGCCTGGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A9S1
UniProtKB Entry NameFUCO_ECOLI
GenBank Gene IDM31059
General References
  1. Chen YM, Lu Z, Lin EC: Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol. J Bacteriol. 1989 Nov;171(11):6097-105. [Article]
  2. Lu Z, Lin EC: The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation. Nucleic Acids Res. 1989 Jun 26;17(12):4883-4. [Article]
  3. Conway T, Ingram LO: Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J Bacteriol. 1989 Jul;171(7):3754-9. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Shao Z, Newman EB: Sequencing and characterization of the sdaB gene from Escherichia coli K-12. Eur J Biochem. 1993 Mar 15;212(3):777-84. [Article]
  7. Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J: Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli. J Bacteriol. 2005 Jul;187(14):4957-66. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02059Adenosine-5-DiphosphoriboseexperimentalunknownDetails