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Protein

2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase

Gene

mhpC

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

Functioni

Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain.3 Publications

Miscellaneous

MhpC is not a serine hydrolase (catalytic triad), as Ser-114 is a non-nucleophilic catalytic residue and Asp-239 is not involved in the catalytic mechanism.

Catalytic activityi

(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate.1 Publication
(2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + fumarate.1 Publication

Kineticsi

Kcat is 28 sec(-1) for hydrolase activity with 2-hydroxy-6-oxononadienedioate as substrate.1 Publication
  1. KM=2.1 µM for 2-hydroxy-6-oxononadienedioate (at pH 8)1 Publication
  2. KM=6.8 µM for 2-hydroxy-6-oxononadienedioate (at pH 8)1 Publication

    Pathwayi: 3-phenylpropanoate degradation

    This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei114Transition state stabilizer1 Publication1
    Sitei192Catalytic role in ketonization of the dienol substrate (substrate destabilization)2 Publications1
    Active sitei267Proton acceptor1 Publication1

    GO - Molecular functioni

    • 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity Source: EcoCyc
    • 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity Source: EcoCyc
    • hydrolase activity Source: EcoliWiki
    • protein homodimerization activity Source: InterPro

    GO - Biological processi

    • 3-(3-hydroxy)phenylpropionate catabolic process Source: EcoCyc
    • 3-phenylpropionate catabolic process Source: UniProtKB-UniPathway
    • aromatic compound catabolic process Source: EcoliWiki

    Keywordsi

    Molecular functionHydrolase
    Biological processAromatic hydrocarbons catabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:MHPCHYDROL-MONOMER
    MetaCyc:MHPCHYDROL-MONOMER
    BRENDAi3.7.1.14 2026
    UniPathwayiUPA00714

    Protein family/group databases

    ESTHERiecoli-mhpc Carbon-carbon_bond_hydrolase
    MEROPSiS33.995

    Chemistry databases

    SwissLipidsiSLP:000001887

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase (EC:3.7.1.141 Publication)
    Alternative name(s):
    2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase
    2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase
    2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase
    Gene namesi
    Name:mhpC
    Ordered Locus Names:b0349, JW0340
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG20275 mhpC

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi44S → A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate. 1 Publication1
    Mutagenesisi113N → A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication1
    Mutagenesisi113N → H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication1
    Mutagenesisi114S → A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication1
    Mutagenesisi114S → G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication1
    Mutagenesisi118H → A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity. 1 Publication1
    Mutagenesisi177F → D: 100-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi177F → G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively. 1 Publication1
    Mutagenesisi192R → K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively. 1 Publication1
    Mutagenesisi192R → Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively. 1 Publication1
    Mutagenesisi265C → A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication1
    Mutagenesisi267H → A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage. 1 Publication1
    Mutagenesisi268W → G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00002070542 – 2882-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolaseAdd BLAST287

    Proteomic databases

    PaxDbiP77044
    PRIDEiP77044

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi4260729, 8 interactors
    DIPiDIP-10207N
    IntActiP77044, 3 interactors
    STRINGi316385.ECDH10B_1361

    Structurei

    Secondary structure

    1288
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi8 – 11Combined sources4
    Beta strandi12 – 19Combined sources8
    Beta strandi22 – 31Combined sources10
    Beta strandi35 – 41Combined sources7
    Helixi50 – 53Combined sources4
    Turni54 – 57Combined sources4
    Helixi58 – 63Combined sources6
    Beta strandi67 – 71Combined sources5
    Helixi88 – 102Combined sources15
    Beta strandi108 – 113Combined sources6
    Helixi115 – 126Combined sources12
    Helixi128 – 130Combined sources3
    Beta strandi131 – 138Combined sources8
    Beta strandi146 – 148Combined sources3
    Helixi153 – 163Combined sources11
    Helixi167 – 175Combined sources9
    Helixi186 – 198Combined sources13
    Helixi200 – 212Combined sources13
    Helixi221 – 226Combined sources6
    Beta strandi231 – 236Combined sources6
    Beta strandi240 – 242Combined sources3
    Helixi245 – 253Combined sources9
    Beta strandi258 – 264Combined sources7
    Helixi269 – 272Combined sources4
    Helixi274 – 285Combined sources12

    3D structure databases

    ProteinModelPortaliP77044
    SMRiP77044
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77044

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. MhpC family.Curated

    Phylogenomic databases

    eggNOGiENOG4106HB6 Bacteria
    COG0596 LUCA
    HOGENOMiHOG000028063
    InParanoidiP77044
    KOiK05714

    Family and domain databases

    Gene3Di3.40.50.1820, 1 hit
    HAMAPiMF_01654 MhpC, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR000073 AB_hydrolase_1
    IPR000639 Epox_hydrolase-like
    IPR023791 MhpC_alpha/beta_hydrolase
    PfamiView protein in Pfam
    PF12697 Abhydrolase_6, 1 hit
    PRINTSiPR00111 ABHYDROLASE
    PR00412 EPOXHYDRLASE
    SUPFAMiSSF53474 SSF53474, 1 hit

    Sequencei

    Sequence statusi: Complete.

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

    P77044-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG
    60 70 80 90 100
    WANFSRNIDP LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV
    110 120 130 140 150
    DQLDIAKIHL LGNSMGGHSS VAFTLKWPER VGKLVLMGGG TGGMSLFTPM
    160 170 180 190 200
    PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD TSDLTDALFE ARLNNMLSRR
    210 220 230 240 250
    DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR FVPMDAGLRL
    260 270 280
    LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP
    Length:288
    Mass (Da):31,937
    Last modified:December 14, 2011 - v4
    Checksum:i8F7E5ADE584A45BA
    GO

    Sequence cautioni

    The sequence AAB18073 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA13054 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAE76131 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence CAA70749 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti153E → G in BAA13054 (Ref. 1) Curated1

    Mass spectrometryi

    Molecular mass is 31717 Da from positions 8 - 288. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D86239 Genomic DNA Translation: BAA13054.1 Different initiation.
    Y09555 Genomic DNA Translation: CAA70749.1 Different initiation.
    U73857 Genomic DNA Translation: AAB18073.1 Different initiation.
    U00096 Genomic DNA Translation: AAC73452.3
    AP009048 Genomic DNA Translation: BAE76131.1 Different initiation.
    PIRiE64762
    RefSeqiNP_414883.5, NC_000913.3
    WP_000121907.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73452; AAC73452; b0349
    BAE76131; BAE76131; BAE76131
    GeneIDi944954
    KEGGiecj:JW0340
    eco:b0349
    PATRICifig|1411691.4.peg.1929

    Similar proteinsi

    Entry informationi

    Entry nameiMHPC_ECOLI
    AccessioniPrimary (citable) accession number: P77044
    Secondary accession number(s): P71204, P77205, Q2MC75
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 14, 2011
    Last modified: April 25, 2018
    This is version 142 of the entry and version 4 of the sequence. See 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

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