LPXA_CYACA
ID LPXA_CYACA Reviewed; 269 AA.
AC Q9TLX4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387};
OS Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that in bacteria anchors the lipopolysaccharide to the outer
CC membrane of the cell. The target for the lipopolysaccharides produced
CC in the chloroplast could either be the cell envelope of the eukaryote
CC or the plastid membrane. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00387};
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 1/6. {ECO:0000255|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR EMBL; AF022186; AAF12950.1; -; Genomic_DNA.
DR RefSeq; NP_045144.1; NC_001840.1.
DR AlphaFoldDB; Q9TLX4; -.
DR SMR; Q9TLX4; -.
DR GeneID; 800145; -.
DR UniPathway; UPA00359; UER00477.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR HAMAP; MF_00387; LpxA; 1.
DR InterPro; IPR029098; Acetyltransf_C.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR010137; Lipid_A_LpxA.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43480; PTHR43480; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 2.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Chloroplast; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Plastid; Repeat; Transferase.
FT CHAIN 1..269
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_0000188082"
SQ SEQUENCE 269 AA; 29377 MW; 7DC42DD00AD0DF7B CRC64;
MTNIHSTAIV HPAASLGRNV VVGPYSIIGS DVSIGDYTRI GPHVVITGKT VIGCNNQILS
GCILGSVPQD LRYIDSELTG LYIGNNNLIR ENVTVHRASG NGVTYIGNNN LIMVNCHVAH
DCQIRNNIII SNSVSLAGHV IIDSCVIIGG HAGLHQFVHV GALSMIAAMS KIEKNVLPFV
VVSGMPAITR TINLVGLKRY GISKTDINYI RLMLENLKVQ PLAFDTYSIF KKFKSDNLLK
RNVAVQYFSD FLFNSFRARG FIPFKVPKK
