(data stored in ACNUC10821 zone)

SWISSPROT: C8U1G8_ECO10

ID   C8U1G8_ECO10            Unreviewed;       305 AA.
AC   C8U1G8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00904479};
DE            Short=UDP-3-O-acyl-GlcNAc deacetylase {ECO:0000256|HAMAP-Rule:MF_00388};
DE            EC=3.5.1.108 {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00904476};
DE   AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase {ECO:0000256|HAMAP-Rule:MF_00388};
GN   Name=lpxC {ECO:0000256|HAMAP-Rule:MF_00388,
GN   ECO:0000313|EMBL:BAI28976.1};
GN   OrderedLocusNames=ECO103_0098 {ECO:0000313|EMBL:BAI28976.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28976.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28976.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00531485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-
CC         alpha-D-glucosamine = acetate + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine; Xref=Rhea:RHEA:25209,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:61494,
CC         ChEBI:CHEBI:71573; EC=3.5.1.108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00388, ECO:0000256|SAAS:SAAS01120543};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00388, ECO:0000256|SAAS:SAAS00531487};
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:0000256|HAMAP-
CC       Rule:MF_00388, ECO:0000256|SAAS:SAAS00041382}.
CC   -!- SIMILARITY: Belongs to the LpxC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00388, ECO:0000256|SAAS:SAAS00904468}.
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DR   EMBL; AP010958; BAI28976.1; -; Genomic_DNA.
DR   RefSeq; WP_000595482.1; NC_013353.1.
DR   SMR; C8U1G8; -.
DR   EnsemblBacteria; BAI28976; BAI28976; ECO103_0098.
DR   KEGG; eoh:ECO103_0098; -.
DR   HOGENOM; HOG000256663; -.
DR   KO; K02535; -.
DR   OMA; IVFYRSD; -.
DR   BioCyc; ECOL585395:ECO103_RS00495-MONOMER; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000000959; 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; C8U1G8.
DR   SWISS-2DPAGE; C8U1G8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00436291};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00089544};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00436293};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00057649};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00388,
KW   ECO:0000256|SAAS:SAAS00531484};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00388, ECO:0000256|SAAS:SAAS00531488}.
FT   ACT_SITE    265    265       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00388}.
FT   METAL        79     79       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00388}.
FT   METAL       238    238       Zinc; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00388}.
FT   METAL       242    242       Zinc. {ECO:0000256|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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