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Database: UniProt
Entry: H2FXK9_OCESG
LinkDB: H2FXK9_OCESG
Original site: H2FXK9_OCESG 
ID   H2FXK9_OCESG            Unreviewed;       340 AA.
AC   H2FXK9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   ECO:0000313|EMBL:AEY02341.1};
GN   OrderedLocusNames=GU3_12940 {ECO:0000313|EMBL:AEY02341.1};
OS   Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Oceanimonas.
OX   NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY02341.1, ECO:0000313|Proteomes:UP000007742};
RN   [1] {ECO:0000313|EMBL:AEY02341.1, ECO:0000313|Proteomes:UP000007742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GK1 {ECO:0000313|EMBL:AEY02341.1,
RC   ECO:0000313|Proteomes:UP000007742};
RX   PubMed=22461556; DOI=10.1128/JB.00023-12;
RA   Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA   Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT   "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT   from Gavkhouni Wetland in Iran.";
RL   J. Bacteriol. 194:2123-2124(2012).
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}.
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DR   EMBL; CP003171; AEY02341.1; -; Genomic_DNA.
DR   RefSeq; WP_014293050.1; NC_016745.1.
DR   AlphaFoldDB; H2FXK9; -.
DR   STRING; 511062.GU3_12940; -.
DR   KEGG; oce:GU3_12940; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_1_6; -.
DR   OrthoDB; 9784739at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000007742; 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   Gene3D; 1.20.5.170; -; 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; IPR018357; Hexapep_transf_CS.
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.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00523};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007742};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00523};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00523}.
FT   DOMAIN          23..87
FT                   /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT                   acyltransferase non-repeat region"
FT                   /evidence="ECO:0000259|Pfam:PF04613"
FT   ACT_SITE        238
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   340 AA;  35589 MW;  91042552AB7B3BBE CRC64;
     MSITLQQLAQ ALGAELHGDA AQPIHRVNTL DKAGPGEVAF LTDSKYRHLL NDTRASAVIL
     READRAACPV ASLVMSDPYL GFALAAQALD TTPAPAVDIH PSAVVADSAT LGEGVAIGAN
     AVIESGVVLE DGVIVGPGCF VGKNTRLGAG TKLWANVTIY HGVTLGTDCL VQSGTVIGSD
     GFGYANNKGE WIKIPQLGGV VIGNRVEIGA CTTIDRGALE DTRIADNVII DNQCQIAHNV
     QIGYGTAMAG GTVMAGSLKV GKYCIIGGAA VFNGHMEICD GVTITGMSMV MRPITEPGTY
     SSGIPLQPNK EWRKTAARVM RIDDMHKRLS QLEKKLNNND
//
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