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Entry version 120 (22 Apr 2020)
Sequence version 1 (25 Oct 2005)
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Protein

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

Gene

menB

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

Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).UniRule annotation4 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

hydrogencarbonateUniRule annotation1 Publication1 PublicationNote: The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by sulfite and nitrate.1 Publication

<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 620 sec(-1) with o-succinylbenzoyl-CoA as substrate(PubMed:21830810). kcat is 1.24 min(-1) with o-succinylbenzoyl-CoA as substrate (PubMed:23658663). All assays are performed at pH 7.0 at 25 degrees Celsius and in the presence of 20 mM NaHCO3.2 Publications
  1. KM=26 µM for o-succinylbenzoyl-CoA1 Publication
  2. KM=2.8 µM for o-succinylbenzoyl-CoA1 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 6 of the subpathway that synthesizes 1,4-dihydroxy-2-naphthoate from chorismate.UniRule annotation
    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 annotation
    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 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 sitei45SubstrateUniRule annotation2 Publications1
    Binding sitei97SubstrateUniRule annotation1 Publication1
    <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>Sitei97Important for catalysisUniRule annotation1 Publication1
    Binding sitei155SubstrateUniRule annotation2 Publications1
    Binding sitei161SubstrateUniRule annotation1 Publication1
    Binding sitei258Substrate; shared with neighboring subunitUniRule annotation1 Publication1
    Sitei258Important for catalysisUniRule annotation1 Publication1
    Binding sitei273Substrate; shared with neighboring subunitUniRule annotation2 Publications1

    <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: EcoCyc

    <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 functionLyase
    Biological processMenaquinone biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:NAPHTHOATE-SYN-MONOMER
    ECOL316407:JW2257-MONOMER
    MetaCyc:NAPHTHOATE-SYN-MONOMER

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

    More...
    UniPathwayi
    UPA00079
    UPA01057;UER00167

    <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 synthase1 PublicationUniRule annotation (EC:4.1.3.36UniRule annotation4 Publications)
    Short name:
    DHNA-CoA synthase1 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:menBUniRule annotation
    Ordered Locus Names:b2262, JW2257
    <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>Mutagenesisi89K → A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity. 1 Publication1
    Mutagenesisi91R → A: Loss of DHNA-CoA synthase activity. 1 Publication1
    Mutagenesisi97Y → F: Loss of DHNA-CoA synthase activity. 1 Publication1
    Mutagenesisi154Q → A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold. 1 Publication1
    Mutagenesisi156G → D: Loss of DHNA-CoA synthase activity. 2 Publications1
    Mutagenesisi184W → F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold. 1 Publication1
    Mutagenesisi267R → A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity. 1 Publication1
    Mutagenesisi270F → A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity. 1 Publication1
    Mutagenesisi273K → A: Impairs protein folding. 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_00001093251 – 2851,4-dihydroxy-2-naphthoyl-CoA synthaseAdd BLAST285

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P0ABU0

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P0ABU0

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

    More...
    PaxDbi
    P0ABU0

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0ABU0

    <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

    Homohexamer. Dimer of a homotrimer.

    4 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4260504, 18 interactors
    851088, 1 interactor

    Database of interacting proteins

    More...
    DIPi
    DIP-47854N

    Protein interaction database and analysis system

    More...
    IntActi
    P0ABU0, 6 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2262

    <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

    1285
    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
    P0ABU0

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <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>Regioni84 – 89Substrate binding2 Publications6
    Regioni129 – 133Substrate bindingUniRule annotation2 Publications5
    Regioni154 – 156Hydrogencarbonate bindingUniRule annotation1 Publication3

    <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 enoyl-CoA hydratase/isomerase family. MenB subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108IPT Bacteria
    COG0447 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_009834_7_7_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P0ABU0

    KEGG Orthology (KO)

    More...
    KOi
    K01661

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P0ABU0

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.12.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01934 MenB, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR010198 DHNA-CoA_synthase_MenB
    IPR018376 Enoyl-CoA_hyd/isom_CS
    IPR001753 Enoyl-CoA_hydra/iso
    IPR014748 Enoyl-CoA_hydra_C

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43113 PTHR43113, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00378 ECH_1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52096 SSF52096, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01929 menB, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00166 ENOYL_COA_HYDRATASE, 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.

    P0ABU0-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MIYPDEAMLY APVEWHDCSE GFEDIRYEKS TDGIAKITIN RPQVRNAFRP
    60 70 80 90 100
    LTVKEMIQAL ADARYDDNIG VIILTGAGDK AFCSGGDQKV RGDYGGYKDD
    110 120 130 140 150
    SGVHHLNVLD FQRQIRTCPK PVVAMVAGYS IGGGHVLHMM CDLTIAADNA
    160 170 180 190 200
    IFGQTGPKVG SFDGGWGASY MARIVGQKKA REIWFLCRQY DAKQALDMGL
    210 220 230 240 250
    VNTVVPLADL EKETVRWCRE MLQNSPMALR CLKAALNADC DGQAGLQELA
    260 270 280
    GNATMLFYMT EEGQEGRNAF NQKRQPDFSK FKRNP
    Length:285
    Mass (Da):31,633
    Last modified:October 25, 2005 - 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:iC38E7206924408E6
    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
    M93421 Genomic DNA Translation: AAA23682.1
    U00096 Genomic DNA Translation: AAC75322.1
    AP009048 Genomic DNA Translation: BAA16086.1
    L35030 Genomic DNA Translation: AAA24152.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A42714 D64997

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_416765.1, NC_000913.3
    WP_000639996.1, NZ_STEB01000008.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75322; AAC75322; b2262
    BAA16086; BAA16086; BAA16086

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    946747

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2257
    eco:b2262

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|511145.12.peg.2355

    <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
    M93421 Genomic DNA Translation: AAA23682.1
    U00096 Genomic DNA Translation: AAC75322.1
    AP009048 Genomic DNA Translation: BAA16086.1
    L35030 Genomic DNA Translation: AAA24152.1
    PIRiA42714 D64997
    RefSeqiNP_416765.1, NC_000913.3
    WP_000639996.1, NZ_STEB01000008.1

    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
    3T88X-ray2.00A/B/C/D/E/F1-285[»]
    3T89X-ray1.95A/B/C/D/E/F1-285[»]
    4ELSX-ray2.30A/B/C/D/E/F1-285[»]
    4ELWX-ray2.55A/B/C/D/E/F1-285[»]
    4ELXX-ray2.19A/B/C/D/E/F1-285[»]
    4I42X-ray1.85A/B/C/D/E/F/G/H/I/J/K/L1-285[»]
    SMRiP0ABU0
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4260504, 18 interactors
    851088, 1 interactor
    DIPiDIP-47854N
    IntActiP0ABU0, 6 interactors
    STRINGi511145.b2262

    Proteomic databases

    EPDiP0ABU0
    jPOSTiP0ABU0
    PaxDbiP0ABU0
    PRIDEiP0ABU0

    Genome annotation databases

    EnsemblBacteriaiAAC75322; AAC75322; b2262
    BAA16086; BAA16086; BAA16086
    GeneIDi946747
    KEGGiecj:JW2257
    eco:b2262
    PATRICifig|511145.12.peg.2355

    Organism-specific databases

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

    More...
    EchoBASEi
    EB1342

    Phylogenomic databases

    eggNOGiENOG4108IPT Bacteria
    COG0447 LUCA
    HOGENOMiCLU_009834_7_7_6
    InParanoidiP0ABU0
    KOiK01661
    PhylomeDBiP0ABU0

    Enzyme and pathway databases

    UniPathwayiUPA00079
    UPA01057;UER00167
    BioCyciEcoCyc:NAPHTHOATE-SYN-MONOMER
    ECOL316407:JW2257-MONOMER
    MetaCyc:NAPHTHOATE-SYN-MONOMER

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P0ABU0

    Family and domain databases

    Gene3Di1.10.12.10, 1 hit
    HAMAPiMF_01934 MenB, 1 hit
    InterProiView protein in InterPro
    IPR029045 ClpP/crotonase-like_dom_sf
    IPR010198 DHNA-CoA_synthase_MenB
    IPR018376 Enoyl-CoA_hyd/isom_CS
    IPR001753 Enoyl-CoA_hydra/iso
    IPR014748 Enoyl-CoA_hydra_C
    PANTHERiPTHR43113 PTHR43113, 1 hit
    PfamiView protein in Pfam
    PF00378 ECH_1, 1 hit
    SUPFAMiSSF52096 SSF52096, 1 hit
    TIGRFAMsiTIGR01929 menB, 1 hit
    PROSITEiView protein in PROSITE
    PS00166 ENOYL_COA_HYDRATASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    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 nameiMENB_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: P0ABU0
    Secondary accession number(s): P27290
    <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: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: April 22, 2020
    This is version 120 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. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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