(data stored in ACNUC7421 zone)

SWISSPROT: LPXC_ECO57

ID   LPXC_ECO57              Reviewed;         305 AA.
AC   P0A727; P07652;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE            Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
DE            EC=3.5.1.108 {ECO:0000255|HAMAP-Rule:MF_00388};
DE   AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000255|HAMAP-Rule:MF_00388};
GN   Name=lpxC {ECO:0000255|HAMAP-Rule:MF_00388};
GN   OrderedLocusNames=Z0106, ECs0100;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-
CC       acetylglucosamine to form UDP-3-O-myristoylglucosamine and
CC       acetate, the committed step in lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00388}.
CC   -!- CATALYTIC ACTIVITY: UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-
CC       acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3-
CC       hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.
CC       {ECO:0000255|HAMAP-Rule:MF_00388}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00388};
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00388}.
CC   -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00388}.
DR   EMBL; AE005174; AAG54400.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33523.1; -; Genomic_DNA.
DR   PIR; D85492; D85492.
DR   PIR; D90641; D90641.
DR   RefSeq; NP_308127.1; NC_002695.1.
DR   RefSeq; WP_000595482.1; NZ_MWVM01000012.1.
DR   ProteinModelPortal; P0A727; -.
DR   SMR; P0A727; -.
DR   STRING; 155864.Z0106; -.
DR   EnsemblBacteria; AAG54400; AAG54400; Z0106.
DR   EnsemblBacteria; BAB33523; BAB33523; BAB33523.
DR   GeneID; 913579; -.
DR   KEGG; ece:Z0106; -.
DR   KEGG; ecs:ECs0100; -.
DR   PATRIC; fig|386585.9.peg.200; -.
DR   eggNOG; ENOG4105C7C; Bacteria.
DR   eggNOG; COG0774; LUCA.
DR   HOGENOM; HOG000256663; -.
DR   KO; K02535; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity; IEA:InterPro.
DR   GO; GO:0103117; F:UDP-3-O-acyl-N-acetylglucosamine deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1700.10; -; 1.
DR   Gene3D; 3.30.230.20; -; 1.
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   PANTHER; PTHR33694:SF2; PTHR33694:SF2; 1.
DR   Pfam; PF03331; LpxC; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   TIGRFAMs; TIGR00325; lpxC; 1.
PE   3: Inferred from homology;
DR   PRODOM; P0A727.
DR   SWISS-2DPAGE; P0A727.
KW   Complete proteome; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Zinc.
FT   CHAIN         1    305       UDP-3-O-acyl-N-acetylglucosamine
FT                                deacetylase.
FT                                /FTId=PRO_0000191931.
FT   ACT_SITE    265    265       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00388}.
FT   METAL        79     79       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00388}.
FT   METAL       238    238       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00388}.
FT   METAL       242    242       Zinc. {ECO:0000255|HAMAP-Rule:MF_00388}.
SQ   SEQUENCE   305 AA;  33956 MW;  CA439A00813463AB 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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