Lactaldehyde reductase

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	None
Molecular Weight	40513.025
Theoretical pI	4.91
GO Classification	Functions ferrous iron binding lactaldehyde reductase activity Processes rhamnose catabolic process L-fucose catabolic process glycol catabolic process propanediol metabolic process Components cytosol
General Function	Lactaldehyde reductase activity
Specific Function	None
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P0A9S1
UniProtKB Entry Name
Cellular Location	None
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	None
Locus	None
References	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. [2553671 ] 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. [2664711 ] 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. [2661535 ] 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. [9278503 ] 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. [16738553 ] 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. [8385012 ] 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. [15995211 ]

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