(data stored in SCRATCH zone)

SWISSPROT: D3UWG9_XENBS

ID   D3UWG9_XENBS            Unreviewed;       342 AA.
AC   D3UWG9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523};
DE   AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523,
GN   ECO:0000313|EMBL:CBJ79743.1};
GN   OrderedLocusNames=XBJ1_0599 {ECO:0000313|EMBL:CBJ79743.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79743.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79743.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79743.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC       (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP
CC       as the acyl donor. Is involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to
CC       the outer membrane of the cell. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] +
CC         UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosamine; Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:71573, ChEBI:CHEBI:78474, ChEBI:CHEBI:78847;
CC         EC=2.3.1.191; Evidence={ECO:0000256|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523,
CC       ECO:0000256|SAAS:SAAS00760705}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxD subfamily. {ECO:0000256|HAMAP-Rule:MF_00523,
CC       ECO:0000256|SAAS:SAAS00760707}.
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DR   EMBL; FN667741; CBJ79743.1; -; Genomic_DNA.
DR   RefSeq; WP_012987197.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0599; -.
DR   EnsemblBacteria; CBJ79743; CBJ79743; XBJ1_0599.
DR   GeneID; 8830221; -.
DR   KEGG; xbo:XBJ1_0599; -.
DR   PATRIC; fig|406818.4.peg.552; -.
DR   eggNOG; ENOG4105D7M; Bacteria.
DR   eggNOG; COG1044; LUCA.
DR   HOGENOM; HOG000294339; -.
DR   KO; K02536; -.
DR   OMA; GFGYAHT; -.
DR   BioCyc; XBOV406818:XBJ1_RS02605-MONOMER; -.
DR   UniPathway; UPA00359; UER00479.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043764; F:UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03352; LbH_LpxD; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   PANTHER; PTHR43378; PTHR43378; 1.
DR   Pfam; PF00132; Hexapep; 3.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE   3: Inferred from homology;
DR   PRODOM; D3UWG9.
DR   SWISS-2DPAGE; D3UWG9.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760710, ECO:0000313|EMBL:CBJ79743.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760688};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760725};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760733};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS01103315};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000256|SAAS:SAAS00760702, ECO:0000313|EMBL:CBJ79743.1}.
FT   DOMAIN       22     88       LpxD. {ECO:0000259|Pfam:PF04613}.
FT   COILED      316    342       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    239    239       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00523}.
SQ   SEQUENCE   342 AA;  36321 MW;  F324C80D0F2DB71F CRC64;
     MVSIRLADLA QQLNAQLHGD GDIVITSIAP MYSANSEQIT FLSDSRYTDK LAECQAAAVV
     LRESDLTHCK VAALVVDNPY LAYARMAQIM DTTPQPAQDI HPSAVIFSEV QLGKNVAVGA
     NAVVESGVIL GDNVIVGAGC FIGKNTRIGA GTRLWANVSV YHNVEIGEQC LIQSGTVIGS
     DGFGYANDRG NWIKIPQLGS VVIGDRVEIG ASTTIDRGAL DNTVIGNGVI IDNQCQIAHN
     VIIGDNTAVA GGVTMAGSLK IGRYCMIGGA SVINGHIEIC DKVTVTGMGM VMRPITEPGV
     YSSGIPLQPN KVWRKTAALV MNINEMNKRL KSVERQREGE NE
//

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