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Database: UniProt
Entry: G9ZJ05_9GAMM
LinkDB: G9ZJ05_9GAMM
Original site: G9ZJ05_9GAMM 
ID   G9ZJ05_9GAMM            Unreviewed;       324 AA.
AC   G9ZJ05;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000256|HAMAP-Rule:MF_00523};
GN   Name=lpxD {ECO:0000256|HAMAP-Rule:MF_00523};
GN   ORFNames=HMPREF9080_02774 {ECO:0000313|EMBL:EHM50585.1};
OS   Cardiobacterium valvarum F0432.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Cardiobacterium.
OX   NCBI_TaxID=797473 {ECO:0000313|EMBL:EHM50585.1, ECO:0000313|Proteomes:UP000004750};
RN   [1] {ECO:0000313|EMBL:EHM50585.1, ECO:0000313|Proteomes:UP000004750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0432 {ECO:0000313|EMBL:EHM50585.1,
RC   ECO:0000313|Proteomes:UP000004750};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00523}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM50585.1}.
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DR   EMBL; AGCM01000178; EHM50585.1; -; Genomic_DNA.
DR   RefSeq; WP_006986758.1; NZ_JH417966.1.
DR   AlphaFoldDB; G9ZJ05; -.
DR   STRING; 797473.HMPREF9080_02774; -.
DR   PATRIC; fig|797473.3.peg.2256; -.
DR   HOGENOM; CLU_049865_0_1_6; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000004750; Unassembled WGS sequence.
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   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   NCBIfam; TIGR01853; lipid_A_lpxD; 1.
DR   PANTHER; PTHR43378; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43378:SF2; UDP-3-O-ACYLGLUCOSAMINE N-ACYLTRANSFERASE 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW   ECO:0000313|EMBL:EHM50585.1};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00523, ECO:0000313|EMBL:EHM50585.1}.
FT   DOMAIN          23..84
FT                   /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT                   acyltransferase non-repeat region"
FT                   /evidence="ECO:0000259|Pfam:PF04613"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   324 AA;  33343 MW;  548E0014282B18E1 CRC64;
     MKTSAGDIAA RLGGILHGDP ATPIHGVGTL QDGQAGEIGF LADAHYRQYL PASRLAAILV
     AEACPEAPMT QIIVKDVKRA WRHLTDGFAP PPPAPAISPQ AHIDPCATLG TNVSIGAGAV
     IGAGADIGDG CRIAPLAYIA DGVTIGRDSN IGSGVRILEK TTIGARANIL ANAVIGERGF
     GNNFEDGRWL PVAQLGGVRI GDDVEIGACT TIDRGAVSDT IIGNGVKLDN HIQIGHNVRI
     GDHTVIAGSA VIAGSVTFGR YCVVGGACVF TGHITICDGA QFTGHSSISK SIHQPGAYSS
     GIPAMPALQW KKFFAKLKLL AKEK
//
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