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    ulaD 3-keto-L-gulonate-6-phosphate decarboxylase UlaD [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948714, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ulaD
    Official Full Name
    3-keto-L-gulonate-6-phosphate decarboxylase UlaD
    Primary source
    ECOCYC:G7858
    Locus tag
    b4196
    See related
    ASAP:ABE-0013729
    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
    ECK4192; sgaH; yjfV
    Summary
    The ula divergon is comprised of the two divergent ulaGR and ulaABCDEF operons. [More information is available at EcoGene: EG12496]. 3-keto-L-gulonate 6-phosphate decarboxylase is an enzyme in the pathway of anaerobic L-ascorbate degradation. [More information is available at EcoCyc: G7858].
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    Genomic context

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    Sequence:
    NC_000913.3 (4422186..4422836)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene L-ascorbate specific PTS enzyme IIB component Neighboring gene L-ascorbate specific PTS enzyme IIA component Neighboring gene L-ribulose-5-phosphate 3-epimerase UlaE Neighboring gene L-ribulose-5-phosphate 4-epimerase UlaF Neighboring gene DUF1471 domain-containing protein YjfY

    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. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Yew WS, et al. Biochemistry, 2004 Jun 1. PMID 15157077
    2. Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily. Wise EL, et al. Biochemistry, 2003 Oct 28. PMID 14567674
    3. Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase. Wise E, et al. Biochemistry, 2002 Mar 26. PMID 11900527
    4. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Yew WS, et al. Biochemistry, 2005 Feb 15. PMID 15697206
    5. Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Wise EL, et al. Biochemistry, 2004 Jun 1. PMID 15157078

    See all (17) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on complete protein
      Title: '98 Escherichia coli SWISS-2DPAGE database update.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 3-dehydro-L-gulonate-6-phosphate decarboxylase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 3-dehydro-L-gulonate-6-phosphate decarboxylase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 3-dehydro-L-gulonate-6-phosphate decarboxylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables carboxy-lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables orotidine-5'-phosphate decarboxylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in 'de novo' pyrimidine nucleobase biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in L-ascorbic acid catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in L-ascorbic acid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within L-ascorbic acid catabolic process IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    3-keto-L-gulonate-6-phosphate decarboxylase UlaD
    NP_418617.1

    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
      4422186..4422836
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418617.1 3-keto-L-gulonate-6-phosphate decarboxylase UlaD [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418617.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A3L5H0L2
      Conserved Domains (1) summary
      PRK13306
      Location:1 → 216
      ulaD; 3-dehydro-L-gulonate-6-phosphate decarboxylase
    Nucleotide Protein
    Heading Accession and Version

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