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Protein

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

Gene

lpxD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

Catalytic activityi

(3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-3-O-((3R)-hydroxytetradecanoyl)-alpha-D-glucosamine = UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein].3 Publications

Enzyme regulationi

Inhibited by divalent cations such as Ca2+ and Mg2+.1 Publication

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

    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)
    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
    Active sitei239Proton acceptor1 Publication1
    Sitei290Involved in determining the hydroxyacyl-ACP selectivity1

    GO - Molecular functioni

    GO - Biological processi

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

    Keywordsi

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

    Enzyme and pathway databases

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

    Chemistry databases

    SwissLipidsiSLP:000001884

    Names & Taxonomyi

    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
    Gene namesi
    Name:lpxD
    Synonyms:firA, omsA
    Ordered Locus Names:b0179, JW0174
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10316 lpxD

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoCyc
    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000596692 – 341UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferaseAdd BLAST340

    Proteomic databases

    EPDiP21645
    PaxDbiP21645
    PRIDEiP21645

    Interactioni

    Subunit structurei

    Homotrimer.2 Publications

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4259589, 448 interactors
    DIPiDIP-10124N
    IntActiP21645, 56 interactors
    STRINGi316385.ECDH10B_0159

    Chemistry databases

    BindingDBiP21645

    Structurei

    Secondary structure

    1341
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 12Combined sources7
    Beta strandi16 – 19Combined sources4
    Turni31 – 33Combined sources3
    Beta strandi38 – 41Combined sources4
    Helixi45 – 53Combined sources9
    Beta strandi57 – 61Combined sources5
    Turni63 – 65Combined sources3
    Helixi66 – 68Combined sources3
    Beta strandi71 – 75Combined sources5
    Helixi79 – 89Combined sources11
    Beta strandi177 – 180Combined sources4
    Beta strandi185 – 188Combined sources4
    Beta strandi191 – 194Combined sources4
    Beta strandi201 – 203Combined sources3
    Beta strandi214 – 216Combined sources3
    Beta strandi219 – 221Combined sources3
    Beta strandi223 – 225Combined sources3
    Beta strandi259 – 261Combined sources3
    Beta strandi275 – 279Combined sources5
    Beta strandi281 – 285Combined sources5
    Beta strandi299 – 302Combined sources4
    Helixi310 – 321Combined sources12
    Helixi323 – 337Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP21645
    SMRiP21645
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21645

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiENOG4105D7M Bacteria
    COG1044 LUCA
    HOGENOMiHOG000294339
    InParanoidiP21645
    KOiK02536
    OMAiGFGYAHT
    PhylomeDBiP21645

    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

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:iB0ADFED5B17C649D
    GO

    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_LN832404.1

    Genome annotation databases

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

    Similar proteinsi

    Entry informationi

    Entry nameiLPXD_ECOLI
    AccessioniPrimary (citable) accession number: P21645
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 23, 2007
    Last modified: May 23, 2018
    This is version 154 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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