(data stored in ACNUC1104 zone)

SWISSPROT: D3UWH1_XENBS

ID   D3UWH1_XENBS            Unreviewed;       265 AA.
AC   D3UWH1;
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=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00720086};
DE            Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE            EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01080267};
GN   Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387,
GN   ECO:0000313|EMBL:CBJ79745.1};
GN   OrderedLocusNames=XBJ1_0601 {ECO:0000313|EMBL:CBJ79745.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79745.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79745.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79745.1,
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: 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_00387,
CC       ECO:0000256|SAAS:SAAS00943771}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-
CC         glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};
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 1/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00387, ECO:0000256|SAAS:SAAS01080285}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS00943784}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxA subfamily. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080288}.
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DR   EMBL; FN667741; CBJ79745.1; -; Genomic_DNA.
DR   RefSeq; WP_012987199.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0601; -.
DR   EnsemblBacteria; CBJ79745; CBJ79745; XBJ1_0601.
DR   GeneID; 8830223; -.
DR   KEGG; xbo:XBJ1_0601; -.
DR   PATRIC; fig|406818.4.peg.554; -.
DR   eggNOG; ENOG4105DAF; Bacteria.
DR   eggNOG; COG1043; LUCA.
DR   HOGENOM; HOG000294326; -.
DR   KO; K00677; -.
DR   OMA; ECVTINR; -.
DR   BioCyc; XBOV406818:XBJ1_RS02615-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR   Gene3D; 1.20.1180.10; -; 1.
DR   HAMAP; MF_00387; LpxA; 1.
DR   InterPro; IPR029098; Acetyltransf_C.
DR   InterPro; IPR037157; Acetyltransf_C_sf.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR010137; Lipid_A_LpxA.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43480; PTHR43480; 1.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE   3: Inferred from homology;
DR   PRODOM; D3UWH1.
DR   SWISS-2DPAGE; D3UWH1.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080269, ECO:0000313|EMBL:CBJ79745.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00943803};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080263};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080278};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00720071};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080266, ECO:0000313|EMBL:CBJ79745.1}.
FT   DOMAIN      180    264       Acetyltransf_11. {ECO:0000259|Pfam:
FT                                PF13720}.
SQ   SEQUENCE   265 AA;  28613 MW;  DFF7AEAC3A34F6DF CRC64;
     MIDQTAVIHP SSIVEEGAVI GGNVRIGPFC YIGSQVEIGE GTEVKSHVVI NGITKIGRDN
     QIYQFASIGE VNQDLKYQGE PTRVEIGDRN RIRESASIHR GTVQGGGLTK IGSDNLLMIN
     THIAHDCMIG DRCIIANNGT LGGHVILGDY VIIGGMTAVH QFCQIGSHVM VGGCSGVAQD
     VPPYVIAQGN HATPFGLNIE GLKRRGFDKE SLHAIRNAYK ALYRSGRTLE EARIEIELQT
     ANNPHVKAFS DFLENSAKSS RGIIR
//

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