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UniProtKB - P62623 (ISPH_ECOLI)

Entry version 138 (07 Apr 2021)
Sequence version 1 (19 Jul 2004)
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Protein

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Gene

ispH

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 conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis (PubMed:11818558, PubMed:11418107, PubMed:12706830, PubMed:19569147, PubMed:22137895). In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition (PubMed:22948824).6 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

[4Fe-4S] cluster5 PublicationsNote: Was shown to bind 1 [3Fe-4S] cluster per subunit (PubMed:19569147, PubMed:20080550, PubMed:15469281). However, it initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (PubMed:12706830, PubMed:22137895, PubMed:20080550, PubMed:22687151).6 Publications

<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

Addition of Ca2+, Mg2+, Mn2+, Ni2+, Co2+ or Fe2+ decreases the catalytic activity (PubMed:15469281). Addition of Zn2+ results in complete loss of activity (PubMed:15469281). Is potently inhibited by substrate analogs in which the hydroxy group in HMBPP is replaced by an amino or thiol group (PubMed:22012762).2 Publications

<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

  1. KM=30 µM for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate1 Publication

    pH dependencei

    Optimum pH is 7.0.

    <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: dimethylallyl diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate.1 Publication1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
    This subpathway is part of the pathway dimethylallyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

    Pathwayi: isopentenyl diphosphate biosynthesis via DXP pathway

    This protein is involved in step 6 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.1 Publication1 Publication
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (ispC), 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
    2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD), 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
    3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE), 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
    4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF), 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
    5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG), 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
    6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH), 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
    This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi12Iron-sulfur (4Fe-4S)Combined sources5 Publications1
    <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 sitei41SubstrateCombined sources1 Publication2 Publications1
    Binding sitei74SubstrateCombined sources1 Publication2 Publications1
    Metal bindingi96Iron-sulfur (4Fe-4S)Combined sources5 Publications1
    Binding sitei124SubstrateCombined sources1 Publication2 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 sitei126Proton donor2 Publications1
    Binding sitei167SubstrateCombined sources1 Publication2 Publications1
    Metal bindingi197Iron-sulfur (4Fe-4S)Combined sources5 Publications1
    Binding sitei269SubstrateCombined sources1 Publication2 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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionOxidoreductase
    Biological processIsoprene biosynthesis
    Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		EcoCyc:EG11081-MONOMER
    MetaCyc:EG11081-MONOMER

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

    More...    UniPathwayi    		UPA00056;UER00097
    UPA00059;UER00105

    <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:
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase1 Publication (EC:1.17.7.43 Publications)
    Short name:
    HMBPP reductase1 Publication
    Alternative name(s):
    1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase1 Publication
    <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:ispH1 Publication
    Synonyms:lytB, yaaE
    Ordered Locus Names:b0029, JW0027
    <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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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

    <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

    Cells lacking this gene are viable only if the medium is supplemented with mevalonate or the cells are complemented with an episomal copy of ispH (PubMed:11418107). A conditional E.coli lytB mutant shows that LytB is essential for survival and that depletion of LytB results in cell lysis (PubMed:11717301).2 Publications

    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>Mutagenesisi12C → S: Loss of catalytic activity. 2 Publications1
    Mutagenesisi41H → N: No effect on catalytic activity. 1 Publication1
    Mutagenesisi74H → N: Reduces catalytic activity 2-fold. 1 Publication1
    Mutagenesisi96C → S: Loss of catalytic activity. 2 Publications1
    Mutagenesisi99V → A: No effect on catalytic activity. 1 Publication1
    Mutagenesisi124H → N: Loss of catalytic activity. 1 Publication1
    Mutagenesisi126E → D or Q: Loss of catalytic activity. 2 Publications1
    Mutagenesisi167T → C: Reduces catalytic activity 3-fold. 2 Publications1
    Mutagenesisi167T → S: No effect on catalytic activity. 2 Publications1
    Mutagenesisi197C → S: Loss of catalytic activity. 2 Publications1
    Mutagenesisi225S → C: Loss of catalytic activity. 1 Publication1
    Mutagenesisi227N → Q: Reduces catalytic activity 20-fold. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...    DrugBanki    		DB01785, Dimethylallyl Diphosphate
    DB04714, ISOPENTENYL PYROPHOSPHATE

    <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_00001288121 – 3164-hydroxy-3-methylbut-2-enyl diphosphate reductaseAdd BLAST316

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P62623

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

    More...    PaxDbi    		P62623

    PRoteomics IDEntifications database

    More...    PRIDEi    		P62623

    <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.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		4262917, 331 interactors
    849179, 2 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-35808N

    Protein interaction database and analysis system

    More...    IntActi    		P62623, 7 interactors

    STRING: functional protein association networks

    More...    STRINGi    		511145.b0029

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P62623

    <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

    1316
    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    		P62623

    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    		P62623

    <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>Regioni225 – 227Substrate bindingCombined sources1 Publication2 Publications3

    <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 IspH family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		COG0761, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_027486_1_0_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P62623

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P62623

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd13944, lytB_ispH, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00191, IspH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR003451, LytB/IspH

    The PANTHER Classification System

    More...    PANTHERi    		PTHR30426, PTHR30426, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF02401, LYTB, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00216, ispH_lytB, 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.

    P62623-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQILLANPRG FCAGVDRAIS IVENALAIYG APIYVRHEVV HNRYVVDSLR 
            60         70         80         90        100
    ERGAIFIEQI SEVPDGAILI FSAHGVSQAV RNEAKSRDLT VFDATCPLVT 
           110        120        130        140        150
    KVHMEVARAS RRGEESILIG HAGHPEVEGT MGQYSNPEGG MYLVESPDDV 
           160        170        180        190        200
    WKLTVKNEEK LSFMTQTTLS VDDTSDVIDA LRKRFPKIVG PRKDDICYAT 
           210        220        230        240        250
    TNRQEAVRAL AEQAEVVLVV GSKNSSNSNR LAELAQRMGK RAFLIDDAKD 
           260        270        280        290        300
    IQEEWVKEVK CVGVTAGASA PDILVQNVVA RLQQLGGGEA IPLEGREENI 
           310 
    VFEVPKELRV DIREVD
    Length:316
    Mass (Da):34,775
    Last modified:July 19, 2004 - 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:i0E7B378BD49AB771
    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
    		AY062212 Genomic DNA Translation: AAL38655.1
    X54945 Genomic DNA Translation: CAA38707.1
    U00096 Genomic DNA Translation: AAC73140.1
    AP009048 Genomic DNA Translation: BAB96598.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		JE0403

    NCBI Reference Sequences

    More...    RefSeqi    		NP_414570.1, NC_000913.3
    WP_001166395.1, NZ_SSZK01000004.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAC73140; AAC73140; b0029
    BAB96598; BAB96598; BAB96598

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		58460832
    944777

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		ecj:JW0027
    eco:b0029

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|1411691.4.peg.2256

    <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
    		AY062212 Genomic DNA Translation: AAL38655.1
    X54945 Genomic DNA Translation: CAA38707.1
    U00096 Genomic DNA Translation: AAC73140.1
    AP009048 Genomic DNA Translation: BAB96598.1
    PIRiJE0403
    RefSeqiNP_414570.1, NC_000913.3
    WP_001166395.1, NZ_SSZK01000004.1

    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
    3F7TX-ray1.80A/B1-316[»]
    3KE8X-ray1.70A/B1-316[»]
    3KE9X-ray1.90A/B1-316[»]
    3KEFX-ray1.70A/B1-316[»]
    3KELX-ray1.80A/B1-316[»]
    3KEMX-ray2.00A/B1-316[»]
    3SZLX-ray1.60A/B1-316[»]
    3SZOX-ray1.60A/B1-316[»]
    3SZUX-ray1.40A/B1-316[»]
    3T0FX-ray1.90A/B1-316[»]
    3T0GX-ray2.10A/B1-316[»]
    3URKX-ray1.50A/B1-316[»]
    3UTCX-ray1.90A/B1-316[»]
    3UTDX-ray1.70A/B1-316[»]
    3UV3X-ray1.60A/B1-316[»]
    3UV6X-ray1.70A/B1-316[»]
    3UV7X-ray1.60A/B1-316[»]
    3UWMX-ray1.80A/B1-316[»]
    3ZGLX-ray1.68A/B1-316[»]
    3ZGNX-ray1.95A/B1-316[»]
    4EB3X-ray1.90A/B1-315[»]
    4H4CX-ray1.80A/B1-315[»]
    4H4DX-ray1.35A/B1-315[»]
    4H4EX-ray1.70A/B1-315[»]
    SMRiP62623
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4262917, 331 interactors
    849179, 2 interactors
    DIPiDIP-35808N
    IntActiP62623, 7 interactors
    STRINGi511145.b0029

    Chemistry databases

    BindingDBiP62623
    DrugBankiDB01785, Dimethylallyl Diphosphate
    DB04714, ISOPENTENYL PYROPHOSPHATE

    Proteomic databases

    jPOSTiP62623
    PaxDbiP62623
    PRIDEiP62623

    Genome annotation databases

    EnsemblBacteriaiAAC73140; AAC73140; b0029
    BAB96598; BAB96598; BAB96598
    GeneIDi58460832
    944777
    KEGGiecj:JW0027
    eco:b0029
    PATRICifig|1411691.4.peg.2256

    Organism-specific databases

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

    More...    EchoBASEi    		EB1073

    Phylogenomic databases

    eggNOGiCOG0761, Bacteria
    HOGENOMiCLU_027486_1_0_6
    InParanoidiP62623
    PhylomeDBiP62623

    Enzyme and pathway databases

    UniPathwayiUPA00056;UER00097
    UPA00059;UER00105
    BioCyciEcoCyc:EG11081-MONOMER
    MetaCyc:EG11081-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP62623

    Protein Ontology

    More...    PROi    		PR:P62623

    Family and domain databases

    CDDicd13944, lytB_ispH, 1 hit
    HAMAPiMF_00191, IspH, 1 hit
    InterProiView protein in InterPro
    IPR003451, LytB/IspH
    PANTHERiPTHR30426, PTHR30426, 1 hit
    PfamiView protein in Pfam
    PF02401, LYTB, 1 hit
    TIGRFAMsiTIGR00216, ispH_lytB, 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 nameiISPH_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: P62623
    Secondary accession number(s): P22565
    <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: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: April 7, 2021
    This is version 138 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. 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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