LPXD_PSEAE
ID LPXD_PSEAE Reviewed; 353 AA.
AC Q9HXY6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=PA3646;
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 [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 [2]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
RX PubMed=21795786; DOI=10.1107/s1744309111018811;
RA Badger J., Chie-Leon B., Logan C., Sridhar V., Sankaran B., Zwart P.H.,
RA Nienaber V.;
RT "The structure of LpxD from Pseudomonas aeruginosa at 1.3 A resolution.";
RL Acta Crystallogr. F 67:749-752(2011).
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-
CC hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of
CC lipid A, a phosphorylated glycolipid that anchors the
CC lipopolysaccharide to the outer membrane of the cell.
CC {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC EC=2.3.1.191; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
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DR EMBL; AE004091; AAG07034.1; -; Genomic_DNA.
DR PIR; F83190; F83190.
DR RefSeq; NP_252336.1; NC_002516.2.
DR RefSeq; WP_003098585.1; NZ_QZGE01000001.1.
DR PDB; 3PMO; X-ray; 1.30 A; A=2-353.
DR PDB; 6UEC; X-ray; 2.60 A; A=3-352.
DR PDB; 6UED; X-ray; 1.55 A; A=3-353.
DR PDBsum; 3PMO; -.
DR PDBsum; 6UEC; -.
DR PDBsum; 6UED; -.
DR AlphaFoldDB; Q9HXY6; -.
DR SMR; Q9HXY6; -.
DR STRING; 287.DR97_4293; -.
DR PaxDb; Q9HXY6; -.
DR PRIDE; Q9HXY6; -.
DR EnsemblBacteria; AAG07034; AAG07034; PA3646.
DR GeneID; 880525; -.
DR KEGG; pae:PA3646; -.
DR PATRIC; fig|208964.12.peg.3815; -.
DR PseudoCAP; PA3646; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR InParanoid; Q9HXY6; -.
DR OMA; QIQIAHN; -.
DR PhylomeDB; Q9HXY6; -.
DR BioCyc; PAER208964:G1FZ6-3716-MON; -.
DR BRENDA; 2.3.1.191; 5087.
DR UniPathway; UPA00973; -.
DR PHI-base; PHI:3784; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03352; LbH_LpxD; 1.
DR HAMAP; MF_00523; LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR007691; LpxD.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR PANTHER; PTHR43378; PTHR43378; 1.
DR Pfam; PF00132; Hexapep; 3.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..353
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000059690"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6UEC"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:3PMO"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:3PMO"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:3PMO"
SQ SEQUENCE 353 AA; 36191 MW; 4B6C4D329F63EA35 CRC64;
MMSTLSYTLG QLAAHVGAEV RGDADLPIQG LATLQEAGPA QLSFLANPQY RKYLPESRAG
AVLLTAADAD GFAGTALVVA NPYLAYASLS HLFDRKPKAA AGIHPTAIVA ADAEVDPSAS
VGAYAVIESG ARIGAGVSIG AHCVIGARSV IGEGGWLAPR VTLYHDVTIG ARVSIQSGAV
IGGEGFGFAN EKGVWQKIAQ IGGVTIGDDV EIGANTTIDR GALSDTLIGN GVKLDNQIMI
AHNVQIGDHT AMAACVGISG SAKIGRHCML AGGVGLVGHI EICDNVFVTG MTMVTRSITE
PGSYSSGTAM QPAAEWKKSA ARIRQLDDMA RRLQQLEKRL AAVTSSGDAS SDA
