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Protein

1,4-dihydroxy-2-naphthoyl-CoA hydrolase

Gene

menI

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

Functioni

Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB.3 Publications

Catalytic activityi

1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA.UniRule annotation2 Publications

Kineticsi

kcat is 6.2 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:23564174). kcat is 1.6 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:24992697). kcat is 0.12 sec(-1) with oleoyl-CoA. kcat is 0.62 sec(-1) with myristoyl-CoA. kcat is 0.0044 sec(-1) with acetyl-CoA. kcat is 0.58 sec(-1) with palmitoyl-CoA. kcat is 0.74 sec(-1) with lauroyl-CoA. kcat is 14.8 sec(-1) with 1-hydroxy-2-naphthoyl-CoA. kcat is 5.2 sec(-1) with 4-hydroxybenzoyl-CoA. kcat is 0.3 sec(-1) with hexanoyl-CoA. kcat is 17.7 sec(-1) with benzoyl-CoA. kcat is 12.6 sec(-1) with 3,5-dihydroxybenzoyl-CoA. kcat is 23.2 sec(-1) with 3,4-dihydroxybenzoyl-CoA. kcat is 8.4 sec(-1) with coumaroyl-CoA. kcat is 0.083 sec(-1) with benzoyl-ACP. kcat is 0.5 sec(-1) with beta-methylcrotonyl-CoA. kcat is 93.0 sec(-1) with salicylyl-CoA. kcat is 0.67 sec(-1) with beta-methylmalonyl-CoA. kcat is 0.21 sec(-1) with propionyl-CoA. kcat is 0.0036 sec(-1) with 2,4-dihydroxybenzoyl-EntB.2 Publications
  1. KM=2.5 µM for 1,4-dihydroxy-2-naphthoyl-CoA1 Publication
  2. KM=8 µM for 1,4-dihydroxy-2-naphthoyl-CoA1 Publication
  3. KM=1.3 µM for oleoyl-CoA1 Publication
  4. KM=1.5 µM for myristoyl-CoA1 Publication
  5. KM=1.559 µM for acetyl-CoA1 Publication
  6. KM=1.9 µM for palmitoyl-CoA1 Publication
  7. KM=2.2 µM for lauroyl-CoA1 Publication
  8. KM=8.0 µM for 1-hydroxy-2-naphthoyl-CoA1 Publication
  9. KM=9 µM for 4-hydroxybenzoyl-CoA1 Publication
  10. KM=21 µM for hexanoyl-CoA1 Publication
  11. KM=25 µM for benzoyl-CoA1 Publication
  12. KM=26.5 µM for 3,5-dihydroxybenzoyl-CoA1 Publication
  13. KM=26.9 µM for 3,4-dihydroxybenzoyl-CoA1 Publication
  14. KM=30 µM for coumaroyl-CoA1 Publication
  15. KM=54 µM for benzoyl-ACP1 Publication
  16. KM=69.4 µM for beta-methylcrotonyl-CoA1 Publication
  17. KM=73 µM for salicylyl-CoA1 Publication
  18. KM=115 µM for beta-methylmalonyl-CoA1 Publication
  19. KM=120 µM for propionyl-CoA1 Publication
  20. KM=200 µM for 2,4-dihydroxybenzoyl-EntB1 Publication

    Pathwayi: 1,4-dihydroxy-2-naphthoate biosynthesis

    This protein is involved in step 7 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation2 Publications
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Isochorismate synthase MenF (menF)
    2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
    3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
    4. o-succinylbenzoate synthase (menC)
    5. 2-succinylbenzoate--CoA ligase (menE)
    6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
    7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
    This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

    Pathwayi: menaquinone biosynthesis

    This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation2 Publications
    View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei63Nucleophile or proton acceptor1 PublicationUniRule annotation1
    Binding sitei82Substrate; via carbonyl oxygenUniRule annotation1 Publication1

    GO - Molecular functioni

    • 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity Source: EcoCyc
    • CoA hydrolase activity Source: EcoCyc
    • hydrolase activity Source: EcoCyc

    GO - Biological processi

    • menaquinone biosynthetic process Source: CACAO

    Keywordsi

    Molecular functionHydrolase
    Biological processMenaquinone biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:G6912-MONOMER
    MetaCyc:G6912-MONOMER
    BRENDAi3.1.2.2 2026
    UniPathwayiUPA00079
    UPA01057; UER01033

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,4-dihydroxy-2-naphthoyl-CoA hydrolaseUniRule annotationCurated (EC:3.1.2.28UniRule annotation2 Publications)
    Short name:
    DHNA-CoA hydrolaseUniRule annotationCurated
    Alternative name(s):
    DHNA-CoA thioesterase1 PublicationUniRule annotation
    Gene namesi
    Name:menI1 PublicationUniRule annotation
    Synonyms:ydiI
    Ordered Locus Names:b1686, JW1676
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13968 menI

    Pathology & Biotechi

    Disruption phenotypei

    Deletion results in a significant decrease in menaquinone production.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi48Q → A: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi48Q → N: 51-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi54H → A: 514-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi54H → F: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi63E → A or Q: Loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi63E → D: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi64S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi67S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi68V → M: 10-fold decrease in catalytic efficiency toward lauroyl-CoA. Does not affect catalytic efficiency toward 1,4-dihydroxy-2-naphthoyl-CoA and benzoyl-CoA. 1 Publication1
    Mutagenesisi71Y → A: Does not affect activity. 1 Publication1
    Mutagenesisi89H → A: 156-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi91R → A: 9-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi106H → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi109S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001566781 – 1361,4-dihydroxy-2-naphthoyl-CoA hydrolaseAdd BLAST136

    Proteomic databases

    PaxDbiP77781
    PRIDEiP77781

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi4259131, 25 interactors
    DIPiDIP-11750N
    IntActiP77781, 3 interactors
    STRINGi316385.ECDH10B_1821

    Structurei

    Secondary structure

    1136
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 14Combined sources6
    Turni15 – 18Combined sources4
    Helixi20 – 23Combined sources4
    Beta strandi27 – 31Combined sources5
    Beta strandi36 – 41Combined sources6
    Turni44 – 46Combined sources3
    Beta strandi51 – 53Combined sources3
    Helixi55 – 72Combined sources18
    Beta strandi79 – 89Combined sources11
    Beta strandi95 – 107Combined sources13
    Beta strandi109 – 119Combined sources11
    Beta strandi125 – 136Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1SBKX-ray2.00A/B/C/D1-136[»]
    1VH5X-ray1.34A/B2-136[»]
    1VI8X-ray2.20A/B/C/D/E/F/G/H2-136[»]
    4K49X-ray1.89A/B/C/D1-136[»]
    4K4AX-ray1.89A/B/C/D1-136[»]
    4K4BX-ray1.90A/B/C/D/E/F/G/H1-136[»]
    ProteinModelPortaliP77781
    SMRiP77781
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77781

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni89 – 92Substrate bindingUniRule annotation1 Publication4
    Regioni106 – 111Substrate bindingUniRule annotation1 Publication6

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105KA0 Bacteria
    COG2050 LUCA
    HOGENOMiHOG000066991
    InParanoidiP77781
    KOiK19222
    OMAiKNTLMET
    PhylomeDBiP77781

    Family and domain databases

    HAMAPiMF_01936 MenI, 1 hit
    InterProiView protein in InterPro
    IPR029069 HotDog_dom_sf
    IPR030863 MenI
    IPR003736 PAAI_dom
    IPR006683 Thioestr_dom
    PfamiView protein in Pfam
    PF03061 4HBT, 1 hit
    SUPFAMiSSF54637 SSF54637, 1 hit
    TIGRFAMsiTIGR00369 unchar_dom_1, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P77781-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIWKRKITLE ALNAMGEGNM VGFLDIRFEH IGDDTLEATM PVDSRTKQPF
    60 70 80 90 100
    GLLHGGASVV LAESIGSVAG YLCTEGEQKV VGLEINANHV RSAREGRVRG
    110 120 130
    VCKPLHLGSR HQVWQIEIFD EKGRLCCSSR LTTAIL
    Length:136
    Mass (Da):14,945
    Last modified:February 1, 1997 - v1
    Checksum:iE7B995390E7244C3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74756.1
    AP009048 Genomic DNA Translation: BAA15452.1
    PIRiF64926
    RefSeqiNP_416201.1, NC_000913.3
    WP_000637982.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74756; AAC74756; b1686
    BAA15452; BAA15452; BAA15452
    GeneIDi946190
    KEGGiecj:JW1676
    eco:b1686
    PATRICifig|511145.12.peg.1757

    Similar proteinsi

    Entry informationi

    Entry nameiMENI_ECOLI
    AccessioniPrimary (citable) accession number: P77781
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: February 1, 1997
    Last modified: March 28, 2018
    This is version 137 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

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