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P77044

- MHPC_ECOLI

UniProt

P77044 - MHPC_ECOLI

Protein

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

Gene

mhpC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 4 (14 Dec 2011)
      Previous versions | rss
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    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

    1. 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity Source: EcoCyc
    2. 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity Source: EcoCyc
    3. hydrolase activity Source: EcoliWiki

    GO - Biological processi

    1. 3-(3-hydroxy)phenylpropionate catabolic process Source: EcoCyc
    2. 3-phenylpropionate catabolic process Source: UniProtKB-UniPathway
    3. aromatic compound catabolic process Source: EcoliWiki

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:MHPCHYDROL-MONOMER.
    ECOL316407:JW0340-MONOMER.
    MetaCyc:MHPCHYDROL-MONOMER.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG20275. mhpC.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki

    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 – 114
    Beta strandi12 – 198
    Beta strandi22 – 3110
    Beta strandi35 – 417
    Helixi50 – 534
    Turni54 – 574
    Helixi58 – 636
    Beta strandi67 – 715
    Helixi88 – 10215
    Beta strandi108 – 1136
    Helixi115 – 12612
    Helixi128 – 1303
    Beta strandi131 – 1388
    Beta strandi146 – 1483
    Helixi153 – 16311
    Helixi167 – 1759
    Helixi186 – 19813
    Helixi200 – 21213
    Helixi221 – 2266
    Beta strandi231 – 2366
    Beta strandi240 – 2423
    Helixi245 – 2539
    Beta strandi258 – 2647
    Helixi269 – 2724
    Helixi274 – 28512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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]
    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

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    MSYQPQTEAA TSRFLNVEEA GKTLRIHFND CGQGDETVVL LHGSGPGATG    50
    WANFSRNIDP LVEAGYRVIL LDCPGWGKSD SVVNSGSRSD LNARILKSVV 100
    DQLDIAKIHL LGNSMGGHSS VAFTLKWPER VGKLVLMGGG TGGMSLFTPM 150
    PTEGIKRLNQ LYRQPTIENL KLMMDIFVFD TSDLTDALFE ARLNNMLSRR 200
    DHLENFVKSL EANPKQFPDF GPRLAEIKAQ TLIVWGRNDR FVPMDAGLRL 250
    LSGIAGSELH IFRDCGHWAQ WEHADAFNQL VLNFLARP 288
    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.
    The sequence BAA13054.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAE76131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA70749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

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

    Mass spectrometryi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488643.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73452; AAC73452; b0349.
    BAE76131; BAE76131; BAE76131.
    GeneIDi12931735.
    944954.
    KEGGiecj:Y75_p0338.
    eco:b0349.
    PATRICi32115831. VBIEscCol129921_0357.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi E64762.
    RefSeqi NP_414883.5. NC_000913.3.
    YP_488643.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U2E X-ray 2.10 A/B/C/D 1-288 [» ]
    ProteinModelPortali P77044.
    SMRi P77044. Positions 3-288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10207N.
    IntActi P77044. 3 interactions.
    STRINGi 511145.b0349.

    Protein family/group databases

    MEROPSi S33.995.

    Proteomic databases

    PaxDbi P77044.
    PRIDEi P77044.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73452 ; AAC73452 ; b0349 .
    BAE76131 ; BAE76131 ; BAE76131 .
    GeneIDi 12931735.
    944954.
    KEGGi ecj:Y75_p0338.
    eco:b0349.
    PATRICi 32115831. VBIEscCol129921_0357.

    Organism-specific databases

    EchoBASEi EB4168.
    EcoGenei EG20275. mhpC.

    Phylogenomic databases

    eggNOGi COG0596.
    HOGENOMi HOG000028063.
    KOi K05714.
    OrthoDBi EOG6PS5TK.

    Enzyme and pathway databases

    UniPathwayi UPA00714 .
    BioCyci EcoCyc:MHPCHYDROL-MONOMER.
    ECOL316407:JW0340-MONOMER.
    MetaCyc:MHPCHYDROL-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P77044.
    PROi P77044.

    Gene expression databases

    Genevestigatori P77044.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    HAMAPi MF_01654. MhpC.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR023791. MhpC_alpha/beta_hydrolase.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 124 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