(data stored in SCRATCH9089 zone)

SWISSPROT: LPXC_PASMU

ID   LPXC_PASMU              Reviewed;         305 AA.
AC   Q9CPA5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 109.
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}; OrderedLocusNames=PM0148;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-
CC       acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the
CC       committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_00388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-D-
CC         glucosamine = acetate + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-
CC         D-glucosamine; Xref=Rhea:RHEA:25209, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:61494, ChEBI:CHEBI:71573;
CC         EC=3.5.1.108; Evidence={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 IV(A)
CC       from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC       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; AE004439; AAK02232.1; -; Genomic_DNA.
DR   RefSeq; WP_005723052.1; NC_002663.1.
DR   SMR; Q9CPA5; -.
DR   EnsemblBacteria; AAK02232; AAK02232; PM0148.
DR   KEGG; pmu:PM0148; -.
DR   PATRIC; fig|272843.6.peg.153; -.
DR   eggNOG; ENOG4105C7C; Bacteria.
DR   eggNOG; COG0774; LUCA.
DR   HOGENOM; HOG000256664; -.
DR   KO; K02535; -.
DR   OMA; IVFYRSD; -.
DR   BioCyc; PMUL272843:G1FZ8-156-MONOMER; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000000809; 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:UniProtKB-UniRule.
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-UniRule.
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; PTHR33694; 1.
DR   Pfam; PF03331; LpxC; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   TIGRFAMs; TIGR00325; lpxC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CPA5.
DR   SWISS-2DPAGE; Q9CPA5.
KW   Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..305
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT                   /id="PRO_0000191942"
FT   ACT_SITE        265
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   METAL           79
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   METAL           238
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   METAL           242
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ   SEQUENCE   305 AA;  33947 MW;  C706BC152A252F32 CRC64;
     MIKQRTLKQS IKVTGVGLHS GNKVTLTLRP AMANTGVIYC RTDLNPPVTF PANANAVRDT
     MLCTCLVNEE GVRISTVEHL NAALAGLGID NVIIEVDAPE IPIMDGSASP FIYLLLDAGI
     EEQNAAKKFI RIKQKVRVED GDKWAEFTPY NGFRLDFTID FEHPAIGKDV RNYVMDFSAQ
     AFVQQISRAR TFGFMKDIEY LQSQGLALGG SLDNAIVLDD YRILNEDGLR FKDELVRHKM
     LDAIGDLYMA GYNIIGDFKA YKSGHGLNNK LLRAVLANQE AWEFVTFDDK QAVPHGYEAP
     TQVLI
//

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