(data stored in ACNUC7421 zone)

SWISSPROT: LPXC_SHESH

ID   LPXC_SHESH              Reviewed;         306 AA.
AC   A8FQA5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
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=Ssed_0415;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000821; ABV35028.1; -; Genomic_DNA.
DR   RefSeq; WP_012140765.1; NC_009831.1.
DR   ProteinModelPortal; A8FQA5; -.
DR   SMR; A8FQA5; -.
DR   STRING; 425104.Ssed_0415; -.
DR   EnsemblBacteria; ABV35028; ABV35028; Ssed_0415.
DR   KEGG; sse:Ssed_0415; -.
DR   eggNOG; ENOG4105C7C; Bacteria.
DR   eggNOG; COG0774; LUCA.
DR   HOGENOM; HOG000256663; -.
DR   KO; K02535; -.
DR   OMA; IVFYRSD; -.
DR   OrthoDB; POG091H0292; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000002015; 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; A8FQA5.
DR   SWISS-2DPAGE; A8FQA5.
KW   Complete proteome; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Zinc.
FT   CHAIN         1    306       UDP-3-O-acyl-N-acetylglucosamine
FT                                deacetylase.
FT                                /FTId=PRO_1000080230.
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   306 AA;  33740 MW;  79EA7A0B5EB1913D CRC64;
     MIFQRTVKEM VKTTGVGLHS GNKVTLSIKP APVNTGIVLV RTDLEPAVAI PAKADLVRET
     TMCTALVNDE GVRISTIEHL FAALAGLGID NAVIEVDAPE IPIMDGSASP WVFLLQSVGI
     QEQASAKKYL RIKNTVRVED GDKWAELKPF KGFRVDFAID FNHPEIARSQ QHMVMDFSTS
     AFVRDISRAR TFGFMRDIEY LRANNLALGG SMENAVVLDE YRVLNPDGLR YEDEFVKHKI
     LDAFGDLYVA GYAIVGEFCA FKTGHALNNQ LVRALLAQQD AWELVSFEKD EAPVSFSVPT
     GAAVFT
//

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