(data stored in SCRATCH zone)

HOGENOM: ECOHS_1_PE100

ID   ECOHS_1_PE100                        STANDARD;      PRT;   305 AA.
AC   ECOHS_1_PE100; A7ZW48;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine
DE   deacetylase; EC=3.5.1 -;AltName: Full=UDP-3-O-acyl-GlcNAc deacetylase;
DE   (ECOHS_1.PE100).
GN   Name=lpxC; OrderedLocusNames=EcHS_A0102;
OS   ESCHERICHIA COLI HS.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOHS_1.PE100.
CC       Escherichia coli HS, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:LPXC_ECOHS
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-3-O-(3-hydroxytetradecanoyl)-N-
CC       acetylglucosamine + H(2)O = UDP-3-O-(3-hydroxytetradecanoyl)-
CC       glucosamine + acetate.
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 2/6.
CC   -!- SIMILARITY: Belongs to the lpxC family.
CC   -!- GENE_FAMILY: HOG000256663 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A7ZW48; -.
DR   EMBL; CP000802; ABV04502.1; -; Genomic_DNA.
DR   RefSeq; YP_001456885.1; NC_009800.1.
DR   ProteinModelPortal; A7ZW48; -.
DR   SMR; A7ZW48; 1-300.
DR   STRING; A7ZW48; -.
DR   EnsemblBacteria; EBESCT00000052405; EBESCP00000050390; EBESCG00000051453.
DR   GeneID; 5591066; -.
DR   GenomeReviews; CP000802_GR; EcHS_A0102.
DR   KEGG; ecx:EcHS_A0102; -.
DR   eggNOG; COG0774; -.
DR   GeneTree; EBGT00050000011113; -.
DR   OMA; KAYKSGH; -.
DR   ProtClustDB; PRK13186; -.
DR   GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00388; LpxC; 1; -.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR004463; UDP-acyl_GlcNac_deAcase.
DR   InterPro; IPR011334; UDP-acyl_GlcNac_deAcase_C.
DR   InterPro; IPR015870; UDP-acyl_N-AcGlcN_deAcase_N.
DR   Gene3D; G3DSA:3.30.1700.10; UDP-acyl_N-AcGlcN_deAcase_C; 1.
DR   Gene3D; G3DSA:3.30.230.20; UDP-acyl_N-AcGlcN_deAcase_N; 1.
DR   Pfam; PF03331; LpxC; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
DR   TIGRFAMs; TIGR00325; LpxC; 1.
DR   HOGENOMDNA; ECOHS_1.PE100; -.
KW   Complete proteome; Hydrolase; Lipid A biosynthesis; Lipid synthesis.
SQ   SEQUENCE   305 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIKQRTLKRI VQATGVGLHT GKKVTLTLRP APANTGVIYR RTDLNPPVDF PADAKSVRDT
     MLCTCLVNEH DVRISTVEHL NAALAGLGID NIVIEVNAPE IPIMDGSAAP FVYLLLDAGI
     DELNCAKKFV RIKETVRVED GDKWAEFKPY NGFSLDFTID FNHPAIDSSN QRYAMNFSAD
     AFMRQISRAR TFGFMRDIEY LQSRGLCLGG SFDCAIVVDD YRVLNEDGLR FEDEFVRHKM
     LDAIGDLFMC GHNIIGAFTA YKSGHALNNK LLQAVLAKQE AWEYVTFQDD AELPLAFKAP
     SAVLA
//

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