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Entry version 152 (07 Oct 2020)
Sequence version 1 (01 Feb 1997)
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Protein

1,4-dihydroxy-2-naphthoyl-CoA hydrolase

Gene

menI

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 hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB.3 Publications

<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 6.2 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:23564174). kcat is 1.6 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:24992697). kcat is 0.12 sec(-1) with oleoyl-CoA. kcat is 0.62 sec(-1) with myristoyl-CoA. kcat is 0.0044 sec(-1) with acetyl-CoA. kcat is 0.58 sec(-1) with palmitoyl-CoA. kcat is 0.74 sec(-1) with lauroyl-CoA. kcat is 14.8 sec(-1) with 1-hydroxy-2-naphthoyl-CoA. kcat is 5.2 sec(-1) with 4-hydroxybenzoyl-CoA. kcat is 0.3 sec(-1) with hexanoyl-CoA. kcat is 17.7 sec(-1) with benzoyl-CoA. kcat is 12.6 sec(-1) with 3,5-dihydroxybenzoyl-CoA. kcat is 23.2 sec(-1) with 3,4-dihydroxybenzoyl-CoA. kcat is 8.4 sec(-1) with coumaroyl-CoA. kcat is 0.083 sec(-1) with benzoyl-ACP. kcat is 0.5 sec(-1) with beta-methylcrotonyl-CoA. kcat is 93.0 sec(-1) with salicylyl-CoA. kcat is 0.67 sec(-1) with beta-methylmalonyl-CoA. kcat is 0.21 sec(-1) with propionyl-CoA. kcat is 0.0036 sec(-1) with 2,4-dihydroxybenzoyl-EntB.2 Publications
  1. KM=2.5 µM for 1,4-dihydroxy-2-naphthoyl-CoA1 Publication
  2. KM=8 µM for 1,4-dihydroxy-2-naphthoyl-CoA1 Publication
  3. KM=1.3 µM for oleoyl-CoA1 Publication
  4. KM=1.5 µM for myristoyl-CoA1 Publication
  5. KM=1.559 µM for acetyl-CoA1 Publication
  6. KM=1.9 µM for palmitoyl-CoA1 Publication
  7. KM=2.2 µM for lauroyl-CoA1 Publication
  8. KM=8.0 µM for 1-hydroxy-2-naphthoyl-CoA1 Publication
  9. KM=9 µM for 4-hydroxybenzoyl-CoA1 Publication
  10. KM=21 µM for hexanoyl-CoA1 Publication
  11. KM=25 µM for benzoyl-CoA1 Publication
  12. KM=26.5 µM for 3,5-dihydroxybenzoyl-CoA1 Publication
  13. KM=26.9 µM for 3,4-dihydroxybenzoyl-CoA1 Publication
  14. KM=30 µM for coumaroyl-CoA1 Publication
  15. KM=54 µM for benzoyl-ACP1 Publication
  16. KM=69.4 µM for beta-methylcrotonyl-CoA1 Publication
  17. KM=73 µM for salicylyl-CoA1 Publication
  18. KM=115 µM for beta-methylmalonyl-CoA1 Publication
  19. KM=120 µM for propionyl-CoA1 Publication
  20. KM=200 µM for 2,4-dihydroxybenzoyl-EntB1 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: 1,4-dihydroxy-2-naphthoate biosynthesis

    This protein is involved in step 7 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation2 Publications
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Isochorismate synthase MenF (menF), Isochorismate synthase MenF (menF)
    2. 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD), 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (menD)
    3. 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH), 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (menH)
    4. o-succinylbenzoate synthase (menC), o-succinylbenzoate synthase (menC)
    5. 2-succinylbenzoate--CoA ligase (menE), 2-succinylbenzoate--CoA ligase (menE)
    6. 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB), 1,4-dihydroxy-2-naphthoyl-CoA synthase (menB)
    7. 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI), 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (menI)
    This subpathway is part of the pathway 1,4-dihydroxy-2-naphthoate biosynthesis, which is itself part of Quinol/quinone metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate, the pathway 1,4-dihydroxy-2-naphthoate biosynthesis and in Quinol/quinone metabolism.

    Pathwayi: menaquinone biosynthesis

    This protein is involved in the pathway menaquinone biosynthesis, which is part of Quinol/quinone metabolism.UniRule annotation2 Publications
    View all proteins of this organism that are known to be involved in the pathway menaquinone biosynthesis and in Quinol/quinone metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei63Nucleophile or proton acceptor1 PublicationUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei82Substrate; via carbonyl oxygenUniRule annotation1 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

    • menaquinone biosynthetic process Source: CACAO

    <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 processMenaquinone biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G6912-MONOMER
    MetaCyc:G6912-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.1.2.2, 2026

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

    More...
    UniPathwayi
    UPA00079
    UPA01057;UER01033

    <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:
    1,4-dihydroxy-2-naphthoyl-CoA hydrolaseUniRule annotationCurated (EC:3.1.2.28UniRule annotation2 Publications)
    Short name:
    DHNA-CoA hydrolaseUniRule annotationCurated
    Alternative name(s):
    DHNA-CoA thioesterase1 PublicationUniRule annotation
    <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:menI1 PublicationUniRule annotation
    Synonyms:ydiI
    Ordered Locus Names:b1686, JW1676
    <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

    • cytosol Source: GO_Central

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Deletion results in a significant decrease in menaquinone production.1 Publication

    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>Mutagenesisi48Q → A: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi48Q → N: 51-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi54H → A: 514-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi54H → F: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi63E → A or Q: Loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi63E → D: Almost loss of activity with benzoyl-CoA as substrate. 1 Publication1
    Mutagenesisi64S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi67S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi68V → M: 10-fold decrease in catalytic efficiency toward lauroyl-CoA. Does not affect catalytic efficiency toward 1,4-dihydroxy-2-naphthoyl-CoA and benzoyl-CoA. 1 Publication1
    Mutagenesisi71Y → A: Does not affect activity. 1 Publication1
    Mutagenesisi89H → A: 156-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi91R → A: 9-fold decrease in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi106H → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 1 Publication1
    Mutagenesisi109S → A: Almost no change in catalytic efficiency toward benzoyl-CoA. 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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001566781 – 1361,4-dihydroxy-2-naphthoyl-CoA hydrolaseAdd BLAST136

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P77781

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

    More...
    PaxDbi
    P77781

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P77781

    <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

    Homotetramer. Dimer of dimers.

    UniRule annotation1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4259131, 25 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-11750N

    Protein interaction database and analysis system

    More...
    IntActi
    P77781, 3 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b1686

    <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

    1136
    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
    P77781

    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
    P77781

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni89 – 92Substrate bindingUniRule annotation1 Publication4
    Regioni106 – 111Substrate bindingUniRule annotation1 Publication6

    <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 thioesterase PaaI family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG2050, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_089876_13_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P77781

    KEGG Orthology (KO)

    More...
    KOi
    K19222

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P77781

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01936, MenI, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029069, HotDog_dom_sf
    IPR030863, MenI
    IPR003736, PAAI_dom
    IPR006683, Thioestr_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03061, 4HBT, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF54637, SSF54637, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00369, unchar_dom_1, 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.

    P77781-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIWKRKITLE ALNAMGEGNM VGFLDIRFEH IGDDTLEATM PVDSRTKQPF
    60 70 80 90 100
    GLLHGGASVV LAESIGSVAG YLCTEGEQKV VGLEINANHV RSAREGRVRG
    110 120 130
    VCKPLHLGSR HQVWQIEIFD EKGRLCCSSR LTTAIL
    Length:136
    Mass (Da):14,945
    Last modified:February 1, 1997 - v1
    <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:iE7B995390E7244C3
    GO

    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
    U00096 Genomic DNA Translation: AAC74756.1
    AP009048 Genomic DNA Translation: BAA15452.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F64926

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416201.1, NC_000913.3
    WP_000637982.1, NZ_STEB01000003.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC74756; AAC74756; b1686
    BAA15452; BAA15452; BAA15452

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946190

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW1676
    eco:b1686

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.1757

    <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
    U00096 Genomic DNA Translation: AAC74756.1
    AP009048 Genomic DNA Translation: BAA15452.1
    PIRiF64926
    RefSeqiNP_416201.1, NC_000913.3
    WP_000637982.1, NZ_STEB01000003.1

    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
    1SBKX-ray2.00A/B/C/D1-136[»]
    1VH5X-ray1.34A/B2-136[»]
    1VI8X-ray2.20A/B/C/D/E/F/G/H2-136[»]
    4K49X-ray1.89A/B/C/D1-136[»]
    4K4AX-ray1.89A/B/C/D1-136[»]
    4K4BX-ray1.90A/B/C/D/E/F/G/H1-136[»]
    SMRiP77781
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4259131, 25 interactors
    DIPiDIP-11750N
    IntActiP77781, 3 interactors
    STRINGi511145.b1686

    Proteomic databases

    jPOSTiP77781
    PaxDbiP77781
    PRIDEiP77781

    Genome annotation databases

    EnsemblBacteriaiAAC74756; AAC74756; b1686
    BAA15452; BAA15452; BAA15452
    GeneIDi946190
    KEGGiecj:JW1676
    eco:b1686
    PATRICifig|511145.12.peg.1757

    Organism-specific databases

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

    More...
    EchoBASEi
    EB3725

    Phylogenomic databases

    eggNOGiCOG2050, Bacteria
    HOGENOMiCLU_089876_13_1_6
    InParanoidiP77781
    KOiK19222
    PhylomeDBiP77781

    Enzyme and pathway databases

    UniPathwayiUPA00079
    UPA01057;UER01033
    BioCyciEcoCyc:G6912-MONOMER
    MetaCyc:G6912-MONOMER
    BRENDAi3.1.2.2, 2026

    Miscellaneous databases

    EvolutionaryTraceiP77781

    Protein Ontology

    More...
    PROi
    PR:P77781

    Family and domain databases

    HAMAPiMF_01936, MenI, 1 hit
    InterProiView protein in InterPro
    IPR029069, HotDog_dom_sf
    IPR030863, MenI
    IPR003736, PAAI_dom
    IPR006683, Thioestr_dom
    PfamiView protein in Pfam
    PF03061, 4HBT, 1 hit
    SUPFAMiSSF54637, SSF54637, 1 hit
    TIGRFAMsiTIGR00369, unchar_dom_1, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiMENI_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: P77781
    <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: April 27, 2001
    Last sequence update: February 1, 1997
    Last modified: October 7, 2020
    This is version 152 of the entry and version 1 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, 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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