ID F2IY26_POLGS Unreviewed; 267 AA.
AC F2IY26;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387};
GN OrderedLocusNames=SL003B_2104 {ECO:0000313|EMBL:ADZ70529.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ70529.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ70529.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that anchors the lipopolysaccharide to the outer membrane of
CC the cell. {ECO:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00387}.
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DR EMBL; CP002568; ADZ70529.1; -; Genomic_DNA.
DR RefSeq; WP_013652847.1; NC_015259.1.
DR AlphaFoldDB; F2IY26; -.
DR STRING; 991905.SL003B_2104; -.
DR KEGG; pgv:SL003B_2104; -.
DR PATRIC; fig|991905.3.peg.2157; -.
DR eggNOG; COG1043; Bacteria.
DR HOGENOM; CLU_061249_0_0_5; -.
DR OrthoDB; 9807278at2; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000008130; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1.
DR HAMAP; MF_00387; LpxA; 1.
DR InterPro; IPR029098; Acetyltransf_C.
DR InterPro; IPR037157; Acetyltransf_C_sf.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR010137; Lipid_A_LpxA.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR01852; lipid_A_lpxA; 1.
DR PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 1.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00387}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00387};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00387};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00387}; Reference proteome {ECO:0000313|Proteomes:UP000008130};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00387};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00387}.
FT DOMAIN 176..251
FT /note="UDP N-acetylglucosamine O-acyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13720"
SQ SEQUENCE 267 AA; 28596 MW; B0FD11A9C5EA97B0 CRC64;
MASIHPTAVI EDGAVLADDV RVGPYCTIGS RVTLGAGVVL ESHVVIAGCT TIGPRTHVYP
FASLGHRPQD LKYAGEDTAL EIGADNQIRE HVTMNPGTEG GGGLTRVGDR CLFMVGSHVG
HDCRVGNSAI FANNATLAGH VEVDDFAILG GLSAVRQWSR IGAHAIVGGM TGVEFDVIPF
GSVIGDRARL AGLNLVGLKR RGFPREQIHA LRAAYRALFE TEEGTLRERA RRLAEEQTDE
PLVRMVTDFI LVEGDRRFCT PRSGSDD
//
