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Entry version 152 (26 Feb 2020)
Sequence version 4 (14 Dec 2011)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei114Transition state stabilizer1 Publication1
    Sitei192Catalytic role in ketonization of the dienol substrate (substrate destabilization)2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei267Proton acceptor1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    Biological processAromatic hydrocarbons catabolism

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:MHPCHYDROL-MONOMER
    ECOL316407:JW0340-MONOMER
    MetaCyc:MHPCHYDROL-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.7.1.14 2026

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00714

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    ecoli-mhpc Carbon-carbon_bond_hydrolase

    MEROPS protease database

    More...
    MEROPSi
    S33.995

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001887

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:mhpC
    Ordered Locus Names:b0349, JW0340
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    GO - Cellular componenti

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002070542 – 2882-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolaseAdd BLAST287

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P77044

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P77044

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260729, 8 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10207N

    Protein interaction database and analysis system

    More...
    IntActi
    P77044, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0349

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1288
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P77044

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P77044

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. MhpC family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4106HB6 Bacteria
    COG0596 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_020336_13_2_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P77044

    KEGG Orthology (KO)

    More...
    KOi
    K05714

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1820, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01654 MhpC, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058 AB_hydrolase
    IPR000073 AB_hydrolase_1
    IPR000639 Epox_hydrolase-like
    IPR023791 MhpC_alpha/beta_hydrolase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF12697 Abhydrolase_6, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00111 ABHYDROLASE
    PR00412 EPOXHYDRLASE

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53474 SSF53474, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8F7E5ADE584A45BA
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAB18073 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
    The sequence BAA13054 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
    The sequence BAE76131 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
    The sequence CAA70749 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti153E → G in BAA13054 (Ref. 1) Curated1

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 31717 Da. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    E64762

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414883.5, NC_000913.3
    WP_000121907.1, NZ_SSZK01000061.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73452; AAC73452; b0349
    BAE76131; BAE76131; BAE76131

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    944954

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0340
    eco:b0349

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.1929

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
    WP_000121907.1, NZ_SSZK01000061.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U2EX-ray2.10A/B/C/D1-288[»]
    SMRiP77044
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4260729, 8 interactors
    DIPiDIP-10207N
    IntActiP77044, 3 interactors
    STRINGi511145.b0349

    Chemistry databases

    SwissLipidsiSLP:000001887

    Protein family/group databases

    ESTHERiecoli-mhpc Carbon-carbon_bond_hydrolase
    MEROPSiS33.995

    Proteomic databases

    PaxDbiP77044
    PRIDEiP77044

    Genome annotation databases

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

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB4168

    Phylogenomic databases

    eggNOGiENOG4106HB6 Bacteria
    COG0596 LUCA
    HOGENOMiCLU_020336_13_2_6
    InParanoidiP77044
    KOiK05714

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP77044

    Protein Ontology

    More...
    PROi
    PR:P77044

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMHPC_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P77044
    Secondary accession number(s): P71204, P77205, Q2MC75
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 14, 2011
    Last modified: February 26, 2020
    This is version 152 of the entry and version 4 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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