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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: Annotation score: 5 out of 5-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.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=2.1 µM for 2-hydroxy-6-oxononadienedioate (at pH 8)1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei114 – 1141Transition state stabilizer
    Sitei192 – 1921Catalytic role in ketonization of the dienol substrate (substrate destabilization)
    Active sitei267 – 2671Proton acceptor

    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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:MHPCHYDROL-MONOMER.
    ECOL316407:JW0340-MONOMER.
    MetaCyc:MHPCHYDROL-MONOMER.
    BRENDAi3.7.1.14. 2026.
    UniPathwayiUPA00714.

    Protein family/group databases

    MEROPSiS33.995.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase (EC:3.7.1.14)
    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG20275. mhpC.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441S → A: 2-fold decrease in catalytic efficiency and more than 5-fold increase in affinity for the natural substrate. 1 Publication
    Mutagenesisi113 – 1131N → A: 200-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
    Mutagenesisi113 – 1131N → H: 350-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
    Mutagenesisi114 – 1141S → A: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication
    Mutagenesisi114 – 1141S → G: Weakly active. 3-fold decrease in affinity. Fast ketonisation and slow C-C cleavage. 1 Publication
    Mutagenesisi118 – 1181H → A: More than 2-fold decrease in catalytic efficiency and 3-fold increase affinity. 1 Publication
    Mutagenesisi177 – 1771F → D: 100-fold decrease in catalytic activity. 1 Publication
    Mutagenesisi177 – 1771F → G: 4-fold and 8-fold decrease in catalytic activity and affinity, respectively. 1 Publication
    Mutagenesisi192 – 1921R → K: 40-fold and 5-fold decrease in catalytic activity and affinity, respectively. 1 Publication
    Mutagenesisi192 – 1921R → Q: 280-fold and 10-fold decrease in catalytic activity and affinity, respectively. 1 Publication
    Mutagenesisi265 – 2651C → A: 2-fold decrease in catalytic activity and almost 2-fold increase in affinity. 1 Publication
    Mutagenesisi267 – 2671H → A: Weakly active, 1000-fold decrease in catalytic efficiency. Very slow ketonisation and C-C cleavage. 1 Publication
    Mutagenesisi268 – 2681W → G: 10-fold and 20-fold decrease in catalytic activity and affinity, respectively. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 2882872-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolasePRO_0000207054Add
    BLAST

    Proteomic databases

    PaxDbiP77044.
    PRIDEiP77044.

    Expressioni

    Gene expression databases

    GenevestigatoriP77044.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-10207N.
    IntActiP77044. 3 interactions.
    STRINGi511145.b0349.

    Structurei

    Secondary structure

    1
    288
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114Combined sources
    Beta strandi12 – 198Combined sources
    Beta strandi22 – 3110Combined sources
    Beta strandi35 – 417Combined sources
    Helixi50 – 534Combined sources
    Turni54 – 574Combined sources
    Helixi58 – 636Combined sources
    Beta strandi67 – 715Combined sources
    Helixi88 – 10215Combined sources
    Beta strandi108 – 1136Combined sources
    Helixi115 – 12612Combined sources
    Helixi128 – 1303Combined sources
    Beta strandi131 – 1388Combined sources
    Beta strandi146 – 1483Combined sources
    Helixi153 – 16311Combined sources
    Helixi167 – 1759Combined sources
    Helixi186 – 19813Combined sources
    Helixi200 – 21213Combined sources
    Helixi221 – 2266Combined sources
    Beta strandi231 – 2366Combined sources
    Beta strandi240 – 2423Combined sources
    Helixi245 – 2539Combined sources
    Beta strandi258 – 2647Combined sources
    Helixi269 – 2724Combined sources
    Helixi274 – 28512Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U2EX-ray2.10A/B/C/D1-288[»]
    ProteinModelPortaliP77044.
    SMRiP77044. Positions 3-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77044.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. MhpC family.Curated

    Phylogenomic databases

    eggNOGiCOG0596.
    HOGENOMiHOG000028063.
    InParanoidiP77044.
    KOiK05714.
    OrthoDBiEOG6PS5TK.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_01654. MhpC.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR023791. MhpC_alpha/beta_hydrolase.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    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 AAB18073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA13054.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAE76131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence CAA70749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531E → G in BAA13054 (Ref. 1) Curated

    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.

    Genome annotation databases

    EnsemblBacteriaiAAC73452; AAC73452; b0349.
    BAE76131; BAE76131; BAE76131.
    GeneIDi944954.
    KEGGiecj:Y75_p0338.
    eco:b0349.
    PATRICi32115831. VBIEscCol129921_0357.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U2EX-ray2.10A/B/C/D1-288[»]
    ProteinModelPortaliP77044.
    SMRiP77044. Positions 3-288.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10207N.
    IntActiP77044. 3 interactions.
    STRINGi511145.b0349.

    Protein family/group databases

    MEROPSiS33.995.

    Proteomic databases

    PaxDbiP77044.
    PRIDEiP77044.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73452; AAC73452; b0349.
    BAE76131; BAE76131; BAE76131.
    GeneIDi944954.
    KEGGiecj:Y75_p0338.
    eco:b0349.
    PATRICi32115831. VBIEscCol129921_0357.

    Organism-specific databases

    EchoBASEiEB4168.
    EcoGeneiEG20275. mhpC.

    Phylogenomic databases

    eggNOGiCOG0596.
    HOGENOMiHOG000028063.
    InParanoidiP77044.
    KOiK05714.
    OrthoDBiEOG6PS5TK.

    Enzyme and pathway databases

    UniPathwayiUPA00714.
    BioCyciEcoCyc:MHPCHYDROL-MONOMER.
    ECOL316407:JW0340-MONOMER.
    MetaCyc:MHPCHYDROL-MONOMER.
    BRENDAi3.7.1.14. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP77044.
    PROiP77044.

    Gene expression databases

    GenevestigatoriP77044.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    HAMAPiMF_01654. MhpC.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR023791. MhpC_alpha/beta_hydrolase.
    [Graphical view]
    PfamiPF12697. Abhydrolase_6. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequence of the mhp operon."
      Kawamukai M.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12."
      Ferrandez A., Garcia J.L., Diaz E.
      J. Bacteriol. 179:2573-2581(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A HYDROLASE.
      Strain: K12 / CS520.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Purification, characterization, and stereochemical analysis of a C-C hydrolase: 2-hydroxy-6-keto-nona-2,4-diene-1,9-dioic acid 5,6-hydrolase."
      Lam W.W., Bugg T.D.
      Biochemistry 36:12242-12251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18, FUNCTION AS A HYDROLASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    7. "Catalytic mechanism of C-C hydrolase MhpC from Escherichia coli: kinetic analysis of His263 and Ser110 site-directed mutants."
      Li C., Montgomery M.G., Mohammed F., Li J.-J., Wood S.P., Bugg T.D.H.
      J. Mol. Biol. 346:241-251(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-44; SER-114; HIS-118 AND HIS-267, CATALYTIC MECHANISM.
    8. "Catalytic role for arginine 188 in the C-C hydrolase catalytic mechanism for Escherichia coli MhpC and Burkholderia xenovorans LB400 BphD."
      Li C., Li J.-J., Montgomery M.G., Wood S.P., Bugg T.D.H.
      Biochemistry 45:12470-12479(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-113; PHE-177; ARG-192; CYS-265 AND TRP-268, CATALYTIC MECHANISM.
    9. "The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism."
      Dunn G., Montgomery M.G., Mohammed F., Coker A., Cooper J.B., Robertson T., Garcia J.-L., Bugg T.D.H., Wood S.P.
      J. Mol. Biol. 346:253-265(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-288 IN COMPLEX WITH A NON-CLEAVABLE SUBSTRATE ANALOG, MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiMHPC_ECOLI
    AccessioniPrimary (citable) accession number: P77044
    Secondary accession number(s): P71204, P77205, Q2MC75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 14, 2011
    Last modified: May 27, 2015
    This is version 129 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    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

    External Data

    Dasty 3

    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 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.