(data stored in SCRATCH3701 zone)

SWISSPROT: LPXC_RICTY

ID   LPXC_RICTY              Reviewed;         289 AA.
AC   Q68XB5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 79.
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=RT0246;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03727.1; -; Genomic_DNA.
DR   RefSeq; WP_011190712.1; NC_006142.1.
DR   SMR; Q68XB5; -.
DR   STRING; 257363.RT0246; -.
DR   EnsemblBacteria; AAU03727; AAU03727; RT0246.
DR   KEGG; rty:RT0246; -.
DR   eggNOG; ENOG4105C7C; Bacteria.
DR   eggNOG; COG0774; LUCA.
DR   HOGENOM; HOG000256664; -.
DR   KO; K02535; -.
DR   OMA; IVFYRSD; -.
DR   OrthoDB; 428602at2; -.
DR   BioCyc; RTYP257363:G1G0L-250-MONOMER; -.
DR   UniPathway; UPA00359; UER00478.
DR   Proteomes; UP000000604; 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; Q68XB5.
DR   SWISS-2DPAGE; Q68XB5.
KW   Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Metal-binding; Zinc.
FT   CHAIN           1..289
FT                   /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT                   /id="PRO_0000191952"
FT   ACT_SITE        263
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           236
FT                   /note="Zinc; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT   METAL           240
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ   SEQUENCE   289 AA;  32097 MW;  0E083D1CE37A8137 CRC64;
     MQQSTLLKPV SCYGIGVHTG KRTQLTIEPA KENTGIIFIR TDISSENNYI EASYYNVSDT
     LLSTTISNNH KIQVSTIEHL MAALWGCSID NAVIKIDGPE VPIMDGSSKP FVFMIECAGK
     KLQNAPKKYL KILKEIKVVN KDCELYCTPS EHITVDLTID FSSKAIGKQN LNFGVQESFT
     KNIADARTFG FIKDVEYLKS KGLAQGASFE NAIGIDEHDK VLNPSGLRYA DEFVRHKLLD
     LFGDLYTSGI SIVSAIKGYK TSHAFNNELL HKIFSDTTSY KFVTSNELS
//

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