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Protein

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase

Gene

entA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the transient intermediate 2-hydroxy-3-oxo-4,6-cyclohexadiene-1-carboxylate, which undergoes rapid aromatization to the final product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds with a C3-hydroxyl group such as methyl 2,3-dihydro-2,3-dihydroxybenzoate, methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate, trans-3-hydroxy-2-cyclohexene-1-carboxylate, cis-3-hydroxy-4-cyclohexene-1-carboxylate, cis-3-hydroxycyclohexane-1-carboxylic acid are oxidized to the corresponding ketone products. The stereospecificity of the C3 allylic alcohol group oxidation is 3R in a 1R,3R dihydro substrate. It can also increase the DHB-AMP ligase activity of EntE by interaction EntE.3 Publications

Catalytic activityi

2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH.1 Publication

Enzyme regulationi

Inhibited by cis-2-hydroxy-3-cyclohexen-1-carboxylate, cis-2-hydroxycyclohexane-1-carboxylate and trans-2-hydroxycyclohexane-1-carboxylate.1 Publication

Kineticsi

Kcat is 5550 min(-1) for dehydrogenase activity with 2,3-dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 1380 min(-1) for dehydrogenase activity with cis-3-hydroxy-4-cyclohexene-1-carboxylate as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 1050 min(-1) for dehydrogenase activity with 2,3-dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 1000 min(-1) for dehydrogenase activity with cis-3,5-cyclohexadiene-1,2-diol as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 300 min(-1) for dehydrogenase activity with trans-3-hydroxy-2-cyclohexene-1-carboxylate and cis-3-hydroxycyclohexane-1-carboxylic acid as substrates (at pH 7.4 and 37 degrees Celsius). Kcat is 180 min(-1) for dehydrogenase activity with methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 60 min(-1) for dehydrogenase activity with trans-3,5-cyclohexadiene-1,2-diol and 2-cyclohexen-1-ol as substrates (at pH 7.4 and 37 degrees Celsius). Kcat is 44 min(-1) for dehydrogenase activity with trans-3-hydroxycyclohexane-1-carboxylic acid as substrate (at pH 7.4 and 37 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=0.26 mM for methyl 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37 degrees Celsius)1 Publication
  2. KM=0.3 mM for 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37 degrees Celsius)1 Publication
  3. KM=1.7 mM for methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate (at pH 7.4 and 37 degrees Celsius)1 Publication
  4. KM=1.9 mM for trans-3-hydroxy-2-cyclohexene-1-carboxylate (at pH 7.4 and 37 degrees Celsius)1 Publication
  5. KM=2.8 mM for cis-3-hydroxy-4-cyclohexene-1-carboxylate (at pH 7.4 and 37 degrees Celsius)1 Publication
  6. KM=4.1 mM for cis-3-hydroxycyclohexane-1-carboxylic acid (at pH 7.4 and 37 degrees Celsius)1 Publication
  7. KM=16.5 mM for trans-3,5-cyclohexadiene-1,2-diol (at pH 7.4 and 37 degrees Celsius)1 Publication
  8. KM=25.2 mM for trans-3-hydroxycyclohexane-1-carboxylic acid (at pH 7.4 and 37 degrees Celsius)1 Publication
  9. KM=83.3 mM for 2-cyclohexen-1-ol (at pH 7.4 and 37 degrees Celsius)1 Publication
  10. KM=168 mM for cis-3,5-cyclohexadiene-1,2-diol (at pH 7.4 and 37 degrees Celsius)1 Publication

    Pathwayi: enterobactin biosynthesis

    This protein is involved in the pathway enterobactin biosynthesis, which is part of Siderophore biosynthesis.Curated
    View all proteins of this organism that are known to be involved in the pathway enterobactin biosynthesis and in Siderophore biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei131SubstrateBy similarity1
    Active sitei144Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi9 – 33NADBy similarityAdd BLAST25

    GO - Molecular functioni

    • 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity Source: EcoCyc
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • enterobactin biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Enterobactin biosynthesis

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:ENTA-MONOMER.
    ECOL316407:JW0588-MONOMER.
    MetaCyc:ENTA-MONOMER.
    UniPathwayiUPA00017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase1 Publication (EC:1.3.1.281 Publication)
    Short name:
    DiDHB-DH1 Publication
    Alternative name(s):
    Trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase1 Publication
    Gene namesi
    Name:entA1 Publication
    Ordered Locus Names:b0596, JW0588
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10259. entA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000546591 – 2482,3-dihydro-2,3-dihydroxybenzoate dehydrogenaseAdd BLAST248

    Proteomic databases

    EPDiP15047.
    PaxDbiP15047.
    PRIDEiP15047.

    Expressioni

    Inductioni

    Under conditions of iron deficiency and by the fur protein.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer; dimer of dimers. EntA and EntE interact together.3 Publications

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260984. 134 interactors.
    DIPiDIP-9511N.
    IntActiP15047. 8 interactors.
    STRINGi511145.b0596.

    Structurei

    Secondary structure

    1248
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 12Combined sources6
    Helixi16 – 27Combined sources12
    Beta strandi31 – 37Combined sources7
    Beta strandi45 – 50Combined sources6
    Helixi56 – 69Combined sources14
    Beta strandi75 – 78Combined sources4
    Turni88 – 90Combined sources3
    Helixi93 – 103Combined sources11
    Helixi105 – 121Combined sources17
    Beta strandi125 – 129Combined sources5
    Helixi132 – 134Combined sources3
    Helixi142 – 162Combined sources21
    Helixi163 – 165Combined sources3
    Beta strandi168 – 174Combined sources7
    Helixi215 – 226Combined sources12
    Helixi228 – 230Combined sources3
    Beta strandi237 – 241Combined sources5
    Turni242 – 247Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2FWMX-ray2.00X1-248[»]
    ProteinModelPortaliP15047.
    SMRiP15047.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15047.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105X17. Bacteria.
    COG1028. LUCA.
    InParanoidiP15047.
    KOiK00216.
    OMAiACAREMV.
    PhylomeDBiP15047.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR003560. DHB_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PRINTSiPR01397. DHBDHDRGNASE.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR04316. dhbA_paeA. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15047-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDFSGKNVWV TGAGKGIGYA TALAFVEAGA KVTGFDQAFT QEQYPFATEV
    60 70 80 90 100
    MDVADAAQVA QVCQRLLAET ERLDALVNAA GILRMGATDQ LSKEDWQQTF
    110 120 130 140 150
    AVNVGGAFNL FQQTMNQFRR QRGGAIVTVA SDAAHTPRIG MSAYGASKAA
    160 170 180 190 200
    LKSLALSVGL ELAGSGVRCN VVSPGSTDTD MQRTLWVSDD AEEQRIRGFG
    210 220 230 240
    EQFKLGIPLG KIARPQEIAN TILFLASDLA SHITLQDIVV DGGSTLGA
    Length:248
    Mass (Da):26,250
    Last modified:April 1, 1990 - v1
    Checksum:iE840488335AD317B
    GO

    Sequence cautioni

    The sequence AAB40796 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M24148 Unassigned DNA. Translation: AAA16103.1.
    M24143 Genomic DNA. Translation: AAA76836.1.
    U82598 Genomic DNA. Translation: AAB40796.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73697.1.
    AP009048 Genomic DNA. Translation: BAE76351.1.
    PIRiA91904. DEECDB.
    RefSeqiNP_415128.1. NC_000913.3.
    WP_000347651.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73697; AAC73697; b0596.
    BAE76351; BAE76351; BAE76351.
    GeneIDi945284.
    KEGGiecj:JW0588.
    eco:b0596.
    PATRICi32116368. VBIEscCol129921_0624.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M24148 Unassigned DNA. Translation: AAA16103.1.
    M24143 Genomic DNA. Translation: AAA76836.1.
    U82598 Genomic DNA. Translation: AAB40796.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73697.1.
    AP009048 Genomic DNA. Translation: BAE76351.1.
    PIRiA91904. DEECDB.
    RefSeqiNP_415128.1. NC_000913.3.
    WP_000347651.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2FWMX-ray2.00X1-248[»]
    ProteinModelPortaliP15047.
    SMRiP15047.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260984. 134 interactors.
    DIPiDIP-9511N.
    IntActiP15047. 8 interactors.
    STRINGi511145.b0596.

    Proteomic databases

    EPDiP15047.
    PaxDbiP15047.
    PRIDEiP15047.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73697; AAC73697; b0596.
    BAE76351; BAE76351; BAE76351.
    GeneIDi945284.
    KEGGiecj:JW0588.
    eco:b0596.
    PATRICi32116368. VBIEscCol129921_0624.

    Organism-specific databases

    EchoBASEiEB0255.
    EcoGeneiEG10259. entA.

    Phylogenomic databases

    eggNOGiENOG4105X17. Bacteria.
    COG1028. LUCA.
    InParanoidiP15047.
    KOiK00216.
    OMAiACAREMV.
    PhylomeDBiP15047.

    Enzyme and pathway databases

    UniPathwayiUPA00017.
    BioCyciEcoCyc:ENTA-MONOMER.
    ECOL316407:JW0588-MONOMER.
    MetaCyc:ENTA-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP15047.
    PROiP15047.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR003560. DHB_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    IPR002347. SDR_fam.
    [Graphical view]
    PANTHERiPTHR24322. PTHR24322. 2 hits.
    PRINTSiPR01397. DHBDHDRGNASE.
    PR00080. SDRFAMILY.
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR04316. dhbA_paeA. 1 hit.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiENTA_ECOLI
    AccessioniPrimary (citable) accession number: P15047
    Secondary accession number(s): P77100, Q2MBK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: November 2, 2016
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.