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Entry version 165 (26 Feb 2020)
Sequence version 2 (23 Jan 2007)
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Protein

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

Gene

lpxD

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 N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2' positions.2 Publications

Caution

Was originally thought to be involved in transcription.Curated

<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 <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 divalent cations such as Ca2+ and Mg2+.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 23 sec(-1).
  1. KM=2.5 µM for UDP-3-O-((3R)-hydroxytetradecanoyl)-alpha-D-glucosamine1 Publication
  2. KM=3.2 µM for (3R)-3-hydroxytetradecanoyl-ACP1 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: lipid IV(A) biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
    2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
    3. UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
    4. UDP-2,3-diacylglucosamine hydrolase (lpxH)
    5. Lipid-A-disaccharide synthase (lpxB)
    6. Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK)
    This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

    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 sitei239Proton acceptor1 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>Sitei290Involved in determining the hydroxyacyl-ACP selectivity1

    <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

    • lipid A biosynthetic process Source: EcoliWiki
    • response to antibiotic Source: UniProtKB-KW

    <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 functionAcyltransferase, Transferase
    Biological processAntibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO
    ECOL316407:JW0174-MONOMER
    MetaCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.191 2026

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

    More...
    UniPathwayi
    UPA00359;UER00479

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000001884

    <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:
    UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (EC:2.3.1.191)
    Short name:
    UDP-3-O-(3-OHC14)-GlcN N-acyltransferase
    Alternative name(s):
    Protein FirA
    Rifampicin resistance protein
    UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase
    <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:lpxD
    Synonyms:firA, omsA
    Ordered Locus Names:b0179, JW0174
    <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>Mutagenesisi41F → A: 30-fold decrease in affinity for UDP-3-O-((3R)-hydroxytetradecanoyl)-GlcN and 5-fold decrease in catalytic activity. 1 Publication1
    Mutagenesisi165Q → R in firA200; confers temperature sensitivity and reverses the rifampicin resistance of rpoB mutants. 1 Publication1
    Mutagenesisi172I → F in firA201; confers temperature sensitivity. 1
    Mutagenesisi228G → D in firA200 and firA201; confers temperature sensitivity. 1 Publication1
    Mutagenesisi239H → A: 1000-fold reduction in catalytic activity with very little effect on substrate affinity. 1 Publication1
    Mutagenesisi252G → S in firA200 and firA201; confers temperature sensitivity. 1 Publication1
    Mutagenesisi271S → N in omsA; confers temperature sensitivity. 1 Publication1
    Mutagenesisi276H → A: 30-fold reduction in catalytic activity. 1 Publication1
    Mutagenesisi290M → A: Change in the acyl donor selectivity, showing a preference for 3-hydroxypalmitoyl-ACP over 3-hydroxytetradecanoyl-ACP as substrate. Produces a lipid A with longer acyl chains. 1 Publication1
    Mutagenesisi292M → A: No change in the acyl donor selectivity. 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_00000596692 – 341UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferaseAdd BLAST340

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P21645

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P21645

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

    More...
    PaxDbi
    P21645

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P21645

    <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

    Homotrimer.

    2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259589, 448 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10124N

    Protein interaction database and analysis system

    More...
    IntActi
    P21645, 56 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b0179

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P21645

    <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

    1341
    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
    P21645

    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
    P21645

    <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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105D7M Bacteria
    COG1044 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_049865_0_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P21645

    KEGG Orthology (KO)

    More...
    KOi
    K02536

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P21645

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd03352 LbH_LpxD, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00523 LpxD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001451 Hexapep
    IPR018357 Hexapep_transf_CS
    IPR007691 LpxD
    IPR011004 Trimer_LpxA-like_sf
    IPR020573 UDP_GlcNAc_AcTrfase_non-rep

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR43378 PTHR43378, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00132 Hexapep, 3 hits
    PF14602 Hexapep_2, 1 hit
    PF04613 LpxD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51161 SSF51161, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01853 lipid_A_lpxD, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00101 HEXAPEP_TRANSFERASES, 4 hits

    <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.

    P21645-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPSIRLADLA QQLDAELHGD GDIVITGVAS MQSAQTGHIT FMVNPKYREH
    60 70 80 90 100
    LGLCQASAVV MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI
    110 120 130 140 150
    APSAVIDATA KLGNNVSIGA NAVIESGVEL GDNVIIGAGC FVGKNSKIGA
    160 170 180 190 200
    GSRLWANVTI YHEIQIGQNC LIQSGTVVGA DGFGYANDRG NWVKIPQIGR
    210 220 230 240 250
    VIIGDRVEIG ACTTIDRGAL DDTIIGNGVI IDNQCQIAHN VVIGDNTAVA
    260 270 280 290 300
    GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
    310 320 330 340
    YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KSLERKVNQQ D
    Length:341
    Mass (Da):36,038
    Last modified:January 23, 2007 - v2
    <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:iB0ADFED5B17C649D
    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
    X54797 Genomic DNA Translation: CAA38568.1
    U70214 Genomic DNA Translation: AAB08608.1
    U00096 Genomic DNA Translation: AAC73290.1
    AP009048 Genomic DNA Translation: BAA77854.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S13729

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_414721.1, NC_000913.3
    WP_001139279.1, NZ_STEB01000032.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC73290; AAC73290; b0179
    BAA77854; BAA77854; BAA77854

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    944882

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW0174
    eco:b0179

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.2100

    <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
    X54797 Genomic DNA Translation: CAA38568.1
    U70214 Genomic DNA Translation: AAB08608.1
    U00096 Genomic DNA Translation: AAC73290.1
    AP009048 Genomic DNA Translation: BAA77854.1
    PIRiS13729
    RefSeqiNP_414721.1, NC_000913.3
    WP_001139279.1, NZ_STEB01000032.1

    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
    3EH0X-ray2.60A/B/C1-341[»]
    4IHFX-ray2.10A/B/C/D/E/F3-341[»]
    4IHGX-ray2.89A/B/C/D/E/F3-341[»]
    4IHHX-ray2.13A/B/C/D/E/F3-341[»]
    SMRiP21645
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi4259589, 448 interactors
    DIPiDIP-10124N
    IntActiP21645, 56 interactors
    STRINGi511145.b0179

    Chemistry databases

    BindingDBiP21645
    SwissLipidsiSLP:000001884

    Proteomic databases

    EPDiP21645
    jPOSTiP21645
    PaxDbiP21645
    PRIDEiP21645

    Genome annotation databases

    EnsemblBacteriaiAAC73290; AAC73290; b0179
    BAA77854; BAA77854; BAA77854
    GeneIDi944882
    KEGGiecj:JW0174
    eco:b0179
    PATRICifig|1411691.4.peg.2100

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0312

    Phylogenomic databases

    eggNOGiENOG4105D7M Bacteria
    COG1044 LUCA
    HOGENOMiCLU_049865_0_1_6
    InParanoidiP21645
    KOiK02536
    PhylomeDBiP21645

    Enzyme and pathway databases

    UniPathwayiUPA00359;UER00479
    BioCyciEcoCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO
    ECOL316407:JW0174-MONOMER
    MetaCyc:UDPHYDROXYMYRGLUCOSAMNACETYLTRANS-MONO
    BRENDAi2.3.1.191 2026

    Miscellaneous databases

    EvolutionaryTraceiP21645

    Protein Ontology

    More...
    PROi
    PR:P21645

    Family and domain databases

    CDDicd03352 LbH_LpxD, 1 hit
    HAMAPiMF_00523 LpxD, 1 hit
    InterProiView protein in InterPro
    IPR001451 Hexapep
    IPR018357 Hexapep_transf_CS
    IPR007691 LpxD
    IPR011004 Trimer_LpxA-like_sf
    IPR020573 UDP_GlcNAc_AcTrfase_non-rep
    PANTHERiPTHR43378 PTHR43378, 1 hit
    PfamiView protein in Pfam
    PF00132 Hexapep, 3 hits
    PF14602 Hexapep_2, 1 hit
    PF04613 LpxD, 1 hit
    SUPFAMiSSF51161 SSF51161, 1 hit
    TIGRFAMsiTIGR01853 lipid_A_lpxD, 1 hit
    PROSITEiView protein in PROSITE
    PS00101 HEXAPEP_TRANSFERASES, 4 hits

    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 nameiLPXD_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: P21645
    <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: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: February 26, 2020
    This is version 165 of the entry and version 2 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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