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    fucO L-1,2-propanediol oxidoreductase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947273, updated on 17-Dec-2024

    Summary

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    Official Symbol
    fucO
    Official Full Name
    L-1,2-propanediol oxidoreductase
    Primary source
    ECOCYC:EG10351
    Locus tag
    b2799
    See related
    ASAP:ABE-0009177
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK2794
    Summary
    L-1,2-propanediol oxidoreductase is an iron-dependent group III dehydrogenase. [More information is available at EcoCyc: EG10351].
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    Genomic context

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    Sequence:
    NC_000913.3 (2931865..2933013, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene L-serine deaminase II Neighboring gene flap endonuclease Neighboring gene L-fuculose-phosphate aldolase Neighboring gene L-fucose:H(+) symporter

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Dual control of a common L-1,2-propanediol oxidoreductase by L-fucose and L-rhamnose in Escherichia coli. Chen YM, et al. J Bacteriol, 1984 Mar. PMID 6421801, Free PMC Article
    2. Rhamnose-induced propanediol oxidoreductase in Escherichia coli: purification, properties, and comparison with the fucose-induced enzyme. Boronat A, et al. J Bacteriol, 1979 Nov. PMID 40956, Free PMC Article
    3. Evolution of propanediol utilization in Escherichia coli: mutant with improved substrate-scavenging power. Hacking AJ, et al. J Bacteriol, 1978 Nov. PMID 361712, Free PMC Article
    4. Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation. Cabiscol E, et al. Biochim Biophys Acta, 1992 Jan 9. PMID 1730033
    5. Ferrous-activated nicotinamide adenine dinucleotide-linked dehydrogenase from a mutant of Escherichia coli capable of growth on 1, 2-propanediol. Sridhara S, et al. J Bacteriol, 1969 Apr. PMID 4306747, Free PMC Article

    See all (38) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Beneficial base substitutions in Escherichia coli fucO gene for enhancement of glycolic acid production.
      Title: Beneficial base substitutions in Escherichia coli fucO gene for enhancement of glycolic acid production.
    2. Analyzed effects of mutations inserted during directed evolution of FucO. Kinetic properties of evolved variants have been determined and the observed differences have been rationalized by modeling the tertiary structures of variant and wild-type enzyme.
      Title: Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution.
    3. Expression of fucO from plasmids was shown to increase furfural tolerance by 50% and to permit the fermentation of 15 mM furfural.
      Title: Increased furfural tolerance due to overexpression of NADH-dependent oxidoreductase FucO in Escherichia coli strains engineered for the production of ethanol and lactate.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables R-lactaldehyde reductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables S-lactaldehyde reductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables alcohol dehydrogenase (NAD+) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ferrous iron binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lactaldehyde reductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lactaldehyde reductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within L-fucose catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in fucose catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in fucose metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within glycol catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within propanediol metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within rhamnose catabolic process IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    L-1,2-propanediol oxidoreductase
    NP_417279.2

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      2931865..2933013 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417279.2 L-1,2-propanediol oxidoreductase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417279.2

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A0H3PMT5, A0A1X3I2X7, A0A1X3JDI6, A0A478L4Q9, A0A829LDK6, A0A8E0FN31, A0AAN1VLM7, A0AAN3MCE6, A0AAN3V4M8, B7LEX9, B7N733, C3SWX2
      Conserved Domains (1) summary
      PRK10624
      Location:1 → 382
      PRK10624; L-1,2-propanediol oxidoreductase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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