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Protein

Hydroxycinnamoyl-CoA hydratase-lyase

Gene
N/A
Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde).1 Publication

Catalytic activityi

4-hydroxy-3-methoxyphenyl-beta-hydroxypropanoyl-CoA = feruloyl-CoA + H2O.1 Publication
3-hydroxy-3-(4-hydroxy-3-methoxyphenyl)propanoyl-CoA = vanillin + acetyl-CoA.1 Publication

Kineticsi

kcat is 3.72 sec(-1) with ferulic acid as substrate.

  1. KM=0.0118 mM for ferulic acid1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei29Coenzyme A1
    Binding sitei75Substrate1
    Binding sitei120Coenzyme A; via carbonyl oxygen1
    Binding sitei151Substrate; via carbonyl oxygen1
    Binding sitei239Substrate1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Enzyme and pathway databases

    BRENDAi4.2.1.101. 5121.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxycinnamoyl-CoA hydratase-lyase (EC:4.1.2.41, EC:4.2.1.101)
    Short name:
    HCHL
    Alternative name(s):
    P-hydroxycinnamoyl CoA hydratase/lyase
    Trans-feruloyl-CoA hydratase/vanillin synthase
    OrganismiPseudomonas fluorescens
    Taxonomic identifieri294 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi123S → A: Reduced kcat compared to wild-type but not markerdly. 1 Publication1
    Mutagenesisi143E → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi239Y → F: Increased KM but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004187272 – 276Hydroxycinnamoyl-CoA hydratase-lyaseAdd BLAST275

    Interactioni

    Subunit structurei

    Homohexamer; dimer of trimers.2 Publications

    Protein-protein interaction databases

    STRINGi1114970.PSF113_2659.

    Structurei

    Secondary structure

    1276
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi9 – 16Combined sources8
    Beta strandi18 – 24Combined sources7
    Helixi27 – 29Combined sources3
    Helixi35 – 49Combined sources15
    Beta strandi54 – 62Combined sources9
    Beta strandi65 – 67Combined sources3
    Helixi72 – 81Combined sources10
    Helixi86 – 98Combined sources13
    Turni99 – 104Combined sources6
    Beta strandi109 – 113Combined sources5
    Beta strandi115 – 118Combined sources4
    Helixi119 – 121Combined sources3
    Helixi122 – 127Combined sources6
    Beta strandi128 – 134Combined sources7
    Beta strandi138 – 140Combined sources3
    Helixi142 – 146Combined sources5
    Helixi154 – 161Combined sources8
    Helixi164 – 173Combined sources10
    Beta strandi176 – 178Combined sources3
    Helixi179 – 184Combined sources6
    Beta strandi187 – 192Combined sources6
    Helixi194 – 209Combined sources16
    Helixi213 – 226Combined sources14
    Helixi231 – 248Combined sources18

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J5IX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L1-276[»]
    2VSSX-ray2.22A/B/C/D/E/F1-276[»]
    2VSUX-ray1.90A/B/C/D/E/F1-276[»]
    ProteinModelPortaliO69762.
    SMRiO69762.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO69762.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni70 – 72Coenzyme A binding3
    Regioni142 – 146Coenzyme A binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4108D7R. Bacteria.
    ENOG410XPS4. LUCA.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O69762-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTYEGRWKT VKVEIEDGIA FVILNRPEKR NAMSPTLNRE MIDVLETLEQ
    60 70 80 90 100
    DPAAGVLVLT GAGEAWTAGM DLKEYFREVD AGPEILQEKI RREASQWQWK
    110 120 130 140 150
    LLRMYAKPTI AMVNGWCFGG GFSPLVACDL AICADEATFG LSEINWGIPP
    160 170 180 190 200
    GNLVSKAMAD TVGHRQSLYY IMTGKTFGGQ KAAEMGLVNE SVPLAQLREV
    210 220 230 240 250
    TIELARNLLE KNPVVLRAAK HGFKRCRELT WEQNEDYLYA KLDQSRLLDT
    260 270
    EGGREQGMKQ FLDDKSIKPG LQAYKR
    Length:276
    Mass (Da):31,008
    Last modified:August 1, 1998 - v1
    Checksum:iFDB5AD1539CA7F9A
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti16E → Q AA sequence (PubMed:9461612).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13067 Genomic DNA. Translation: CAA73502.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y13067 Genomic DNA. Translation: CAA73502.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J5IX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L1-276[»]
    2VSSX-ray2.22A/B/C/D/E/F1-276[»]
    2VSUX-ray1.90A/B/C/D/E/F1-276[»]
    ProteinModelPortaliO69762.
    SMRiO69762.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi1114970.PSF113_2659.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4108D7R. Bacteria.
    ENOG410XPS4. LUCA.

    Enzyme and pathway databases

    BRENDAi4.2.1.101. 5121.

    Miscellaneous databases

    EvolutionaryTraceiO69762.

    Family and domain databases

    Gene3Di3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    [Graphical view]
    PfamiPF00378. ECH_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 1 hit.
    PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHCHL_PSEFL
    AccessioniPrimary (citable) accession number: O69762
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: August 1, 1998
    Last modified: November 2, 2016
    This is version 71 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, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.