LPXC_BRUME
ID LPXC_BRUME Reviewed; 286 AA.
AC Q8YI59;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=BMEI0586;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine +
CC H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate;
CC Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108;
CC 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}.
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DR EMBL; AE008917; AAL51767.1; -; Genomic_DNA.
DR PIR; AD3325; AD3325.
DR RefSeq; WP_004684016.1; NZ_GG703780.1.
DR AlphaFoldDB; Q8YI59; -.
DR SMR; Q8YI59; -.
DR STRING; 224914.BMEI0586; -.
DR EnsemblBacteria; AAL51767; AAL51767; BMEI0586.
DR GeneID; 29593377; -.
DR KEGG; bme:BMEI0586; -.
DR PATRIC; fig|224914.52.peg.882; -.
DR eggNOG; COG0774; Bacteria.
DR OMA; IVFYRSD; -.
DR PhylomeDB; Q8YI59; -.
DR UniPathway; UPA00359; UER00478.
DR Proteomes; UP000000419; Chromosome I.
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;
KW Hydrolase; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Zinc.
FT CHAIN 1..286
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT /id="PRO_0000191919"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
SQ SEQUENCE 286 AA; 30867 MW; 90180ACC07F361DE CRC64;
MNAYQKTIGR AVTLSGVGIH GGAPASARLL PADADTGILF QRSDIKDSAP VCAHVSQIGA
TDLCTSLGAR EARIDTVEHL MAAISALGID NLVVEIEGPE VPILDGTSAR FIEAVDSVGV
VTQDAKRRFI RILKTVRVEA GNSWGEFRPY DGTRFEVEID FECPLIGRQK FAHDVDEETF
RKELSTARTF GFMKDVERLW AAGLALGASL DNSLVIGDDN SIVNADGLRF KDEFVRHKTL
DAVGDLALAG LPFIGCFSSY RGGHRLNSEA VKALLSDETA FEIIEA
