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Protein

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

Gene

menI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei63 – 631Nucleophile or proton acceptor1 PublicationUniRule annotation
    Binding sitei82 – 821Substrate; via carbonyl oxygenUniRule annotation1 Publication

    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
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Menaquinone biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:G6912-MONOMER.
    ECOL316407:JW1676-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481Q → A: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication
    Mutagenesisi48 – 481Q → N: 51-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi54 – 541H → A: 514-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi54 – 541H → F: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication
    Mutagenesisi63 – 631E → A or Q: Loss of activity with benzoyl-CoA as substrate. 1 Publication
    Mutagenesisi63 – 631E → D: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication
    Mutagenesisi64 – 641S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi67 – 671S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi68 – 681V → 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 Publication
    Mutagenesisi71 – 711Y → A: Does not affect activity. 1 Publication
    Mutagenesisi89 – 891H → A: 156-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi91 – 911R → A: 9-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi106 – 1061H → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication
    Mutagenesisi109 – 1091S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1361361,4-dihydroxy-2-naphthoyl-CoA hydrolasePRO_0000156678Add
    BLAST

    Proteomic databases

    PaxDbiP77781.
    PRIDEiP77781.

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi4259131. 5 interactions.
    DIPiDIP-11750N.
    IntActiP77781. 2 interactions.
    STRINGi511145.b1686.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 146Combined sources
    Turni15 – 184Combined sources
    Helixi20 – 234Combined sources
    Beta strandi27 – 315Combined sources
    Beta strandi36 – 416Combined sources
    Turni44 – 463Combined sources
    Beta strandi51 – 533Combined sources
    Helixi55 – 7218Combined sources
    Beta strandi79 – 8911Combined sources
    Beta strandi95 – 10713Combined sources
    Beta strandi109 – 11911Combined sources
    Beta strandi125 – 13612Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77781.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni89 – 924Substrate bindingUniRule annotation1 Publication
    Regioni106 – 1116Substrate bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105KA0. Bacteria.
    COG2050. LUCA.
    HOGENOMiHOG000066991.
    InParanoidiP77781.
    KOiK19222.
    OMAiTQVWQID.
    PhylomeDBiP77781.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    HAMAPiMF_01936. MenI. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR030863. MenI.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    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.
    PATRICi32118678. VBIEscCol129921_1757.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259131. 5 interactions.
    DIPiDIP-11750N.
    IntActiP77781. 2 interactions.
    STRINGi511145.b1686.

    Proteomic databases

    PaxDbiP77781.
    PRIDEiP77781.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74756; AAC74756; b1686.
    BAA15452; BAA15452; BAA15452.
    GeneIDi946190.
    KEGGiecj:JW1676.
    eco:b1686.
    PATRICi32118678. VBIEscCol129921_1757.

    Organism-specific databases

    EchoBASEiEB3725.
    EcoGeneiEG13968. menI.

    Phylogenomic databases

    eggNOGiENOG4105KA0. Bacteria.
    COG2050. LUCA.
    HOGENOMiHOG000066991.
    InParanoidiP77781.
    KOiK19222.
    OMAiTQVWQID.
    PhylomeDBiP77781.

    Enzyme and pathway databases

    UniPathwayiUPA00079.
    UPA01057; UER01033.
    BioCyciEcoCyc:G6912-MONOMER.
    ECOL316407:JW1676-MONOMER.
    MetaCyc:G6912-MONOMER.
    BRENDAi3.1.2.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP77781.
    PROiP77781.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    HAMAPiMF_01936. MenI. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR030863. MenI.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_dom.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMENI_ECOLI
    AccessioniPrimary (citable) accession number: P77781
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: February 1, 1997
    Last modified: September 7, 2016
    This is version 127 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, 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.