LPXC_PSEAE
ID LPXC_PSEAE Reviewed; 303 AA.
AC P47205; P97050;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 141.
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, ECO:0000269|PubMed:9068651};
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}; Synonyms=envA;
GN OrderedLocusNames=PA4406;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Levesque R.C.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=ATCC 27853 / DSM 1117 / JCM 6119 / LMG 6395 / NCIMB 12469;
RX PubMed=9068651; DOI=10.1128/jb.179.6.2029-2037.1997;
RA Hyland S.A., Eveland S.S., Anderson M.S.;
RT "Cloning, expression, and purification of UDP-3-O-acyl-GlcNAc deacetylase
RT from Pseudomonas aeruginosa: a metalloamidase of the lipid A biosynthesis
RT pathway.";
RL J. Bacteriol. 179:2029-2037(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8581173; DOI=10.1099/13500872-142-1-79;
RA Liao X., Charlebois I., Ouellet C., Morency M.J., Dewar K., Lightfoot J.,
RA Foster J., Siehnel R., Schweizer H., Lam J.S., Hancock R.E., Levesque R.C.;
RT "Physical mapping of 32 genetic markers on the Pseudomonas aeruginosa PAO1
RT chromosome.";
RL Microbiology 142:79-86(1996).
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, ECO:0000269|PubMed:9068651}.
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 ECO:0000269|PubMed:9068651};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00388,
CC ECO:0000269|PubMed:9068651};
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; U19797; AAA95994.2; -; Genomic_DNA.
DR EMBL; U67855; AAC44974.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07794.1; -; Genomic_DNA.
DR PIR; G83093; G83093.
DR RefSeq; NP_253096.1; NC_002516.2.
DR RefSeq; WP_003094111.1; NZ_QZGE01000004.1.
DR PDB; 2VES; X-ray; 1.90 A; A/B/C=1-299.
DR PDB; 3P3E; X-ray; 1.28 A; A=1-299.
DR PDB; 3U1Y; X-ray; 2.00 A; A/B=1-299.
DR PDB; 3UHM; X-ray; 1.26 A; A=1-299.
DR PDB; 4FW3; X-ray; 2.35 A; A/B/C/D=1-299.
DR PDB; 4FW4; X-ray; 2.19 A; A/B/C/D=1-299.
DR PDB; 4FW5; X-ray; 1.99 A; A/B/C/D=1-299.
DR PDB; 4FW6; X-ray; 1.83 A; A/B/C/D=1-299.
DR PDB; 4FW7; X-ray; 1.70 A; A/B/C/D=1-299.
DR PDB; 4J3D; X-ray; 2.00 A; A/B=1-297.
DR PDB; 4LCF; X-ray; 1.60 A; A=1-299.
DR PDB; 4LCG; X-ray; 1.57 A; A=1-299.
DR PDB; 4LCH; X-ray; 1.60 A; A=1-299.
DR PDB; 4OKG; X-ray; 2.06 A; A/B=1-299.
DR PDB; 5DRQ; X-ray; 1.63 A; A=1-299.
DR PDB; 5DRR; X-ray; 1.59 A; A=1-299.
DR PDB; 5N8C; X-ray; 1.90 A; A/B=1-303.
DR PDB; 5U39; X-ray; 1.75 A; A=2-293.
DR PDB; 5U3B; X-ray; 2.00 A; A/B=1-299.
DR PDB; 5UPG; X-ray; 1.70 A; A=1-303.
DR PDB; 5VWM; X-ray; 1.80 A; A=1-303.
DR PDB; 6C9C; X-ray; 2.00 A; A=1-303.
DR PDB; 6CAX; X-ray; 1.25 A; A=1-303.
DR PDB; 6DUI; X-ray; 1.55 A; A=1-303.
DR PDB; 6E54; X-ray; 1.65 A; A=1-303.
DR PDB; 6I46; X-ray; 1.75 A; AAA=1-299.
DR PDB; 6I47; X-ray; 1.90 A; AAA=1-299.
DR PDB; 6I48; X-ray; 2.20 A; AAA=1-299.
DR PDB; 6I49; X-ray; 1.94 A; AAA/BBB=1-299.
DR PDB; 6I4A; X-ray; 2.25 A; AAA=1-299.
DR PDB; 6MAE; X-ray; 1.80 A; A=1-299.
DR PDB; 6MO4; X-ray; 1.84 A; A=2-299.
DR PDB; 6MO5; X-ray; 1.85 A; A=2-299.
DR PDB; 6MOD; X-ray; 1.85 A; A=2-299.
DR PDB; 6MOO; X-ray; 2.20 A; A=2-299.
DR PDB; 7CI4; X-ray; 2.00 A; A/B=1-299.
DR PDB; 7CI5; X-ray; 2.50 A; A/B/C/D=1-299.
DR PDB; 7CI6; X-ray; 2.70 A; A/B=1-299.
DR PDB; 7CI7; X-ray; 2.10 A; A=1-299.
DR PDB; 7CI8; X-ray; 3.00 A; A/B=1-299.
DR PDB; 7CI9; X-ray; 1.90 A; A=1-299.
DR PDB; 7CIA; X-ray; 1.92 A; A=1-299.
DR PDB; 7CIB; X-ray; 1.61 A; A=1-299.
DR PDB; 7CIC; X-ray; 1.78 A; A/B=1-299.
DR PDB; 7CID; X-ray; 2.49 A; A=1-299.
DR PDB; 7CIE; X-ray; 2.15 A; A/B=1-299.
DR PDB; 7DEL; X-ray; 2.15 A; A=1-299.
DR PDB; 7DEM; X-ray; 1.90 A; A=1-299.
DR PDB; 7DEN; X-ray; 2.07 A; A=1-299.
DR PDB; 7K99; X-ray; 1.90 A; A/C=1-303.
DR PDB; 7K9A; X-ray; 2.00 A; A/C=1-303.
DR PDBsum; 2VES; -.
DR PDBsum; 3P3E; -.
DR PDBsum; 3U1Y; -.
DR PDBsum; 3UHM; -.
DR PDBsum; 4FW3; -.
DR PDBsum; 4FW4; -.
DR PDBsum; 4FW5; -.
DR PDBsum; 4FW6; -.
DR PDBsum; 4FW7; -.
DR PDBsum; 4J3D; -.
DR PDBsum; 4LCF; -.
DR PDBsum; 4LCG; -.
DR PDBsum; 4LCH; -.
DR PDBsum; 4OKG; -.
DR PDBsum; 5DRQ; -.
DR PDBsum; 5DRR; -.
DR PDBsum; 5N8C; -.
DR PDBsum; 5U39; -.
DR PDBsum; 5U3B; -.
DR PDBsum; 5UPG; -.
DR PDBsum; 5VWM; -.
DR PDBsum; 6C9C; -.
DR PDBsum; 6CAX; -.
DR PDBsum; 6DUI; -.
DR PDBsum; 6E54; -.
DR PDBsum; 6I46; -.
DR PDBsum; 6I47; -.
DR PDBsum; 6I48; -.
DR PDBsum; 6I49; -.
DR PDBsum; 6I4A; -.
DR PDBsum; 6MAE; -.
DR PDBsum; 6MO4; -.
DR PDBsum; 6MO5; -.
DR PDBsum; 6MOD; -.
DR PDBsum; 6MOO; -.
DR PDBsum; 7CI4; -.
DR PDBsum; 7CI5; -.
DR PDBsum; 7CI6; -.
DR PDBsum; 7CI7; -.
DR PDBsum; 7CI8; -.
DR PDBsum; 7CI9; -.
DR PDBsum; 7CIA; -.
DR PDBsum; 7CIB; -.
DR PDBsum; 7CIC; -.
DR PDBsum; 7CID; -.
DR PDBsum; 7CIE; -.
DR PDBsum; 7DEL; -.
DR PDBsum; 7DEM; -.
DR PDBsum; 7DEN; -.
DR PDBsum; 7K99; -.
DR PDBsum; 7K9A; -.
DR AlphaFoldDB; P47205; -.
DR SMR; P47205; -.
DR STRING; 287.DR97_1584; -.
DR BindingDB; P47205; -.
DR ChEMBL; CHEMBL3855; -.
DR DrugBank; DB07861; (2R)-N-hydroxy-3-naphthalen-2-yl-2-[(naphthalen-2-ylsulfonyl)amino]propanamide.
DR PaxDb; P47205; -.
DR PRIDE; P47205; -.
DR DNASU; 881292; -.
DR EnsemblBacteria; AAG07794; AAG07794; PA4406.
DR GeneID; 881292; -.
DR KEGG; pae:PA4406; -.
DR PATRIC; fig|208964.12.peg.4615; -.
DR PseudoCAP; PA4406; -.
DR HOGENOM; CLU_046528_1_0_6; -.
DR InParanoid; P47205; -.
DR OMA; IVFYRSD; -.
DR PhylomeDB; P47205; -.
DR BioCyc; PAER208964:G1FZ6-4492-MON; -.
DR BRENDA; 3.5.1.108; 5087.
DR UniPathway; UPA00359; UER00478.
DR EvolutionaryTrace; P47205; -.
DR Proteomes; UP000002438; 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; IDA:PseudoCAP.
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; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..303
FT /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase"
FT /id="PRO_0000191945"
FT ACT_SITE 264
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00388"
FT BINDING 78
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"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3UHM"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3UHM"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:3UHM"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:7CIC"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3UHM"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3UHM"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3UHM"
SQ SEQUENCE 303 AA; 33435 MW; 454403711DCC9B24 CRC64;
MIKQRTLKNI IRATGVGLHS GEKVYLTLKP APVDTGIVFC RTDLDPVVEI PARAENVGET
TMSTTLVKGD VKVDTVEHLL SAMAGLGIDN AYVELSASEV PIMDGSAGPF VFLIQSAGLQ
EQEAAKKFIR IKREVSVEEG DKRAVFVPFD GFKVSFEIDF DHPVFRGRTQ QASVDFSSTS
FVKEVSRART FGFMRDIEYL RSQNLALGGS VENAIVVDEN RVLNEDGLRY EDEFVKHKIL
DAIGDLYLLG NSLIGEFRGF KSGHALNNQL LRTLIADKDA WEVVTFEDAR TAPISYMRPA
AAV
