ID F3ZT08_9BACE Unreviewed; 345 AA.
AC F3ZT08;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=Bcop_0754 {ECO:0000313|EMBL:EGJ70970.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ70970.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ70970.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ70970.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(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: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; CM001167; EGJ70970.1; -; Genomic_DNA.
DR RefSeq; WP_006744126.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZT08; -.
DR STRING; 679937.Bcop_0754; -.
DR eggNOG; COG1044; Bacteria.
DR HOGENOM; CLU_049865_0_0_10; -.
DR OrthoDB; 9784739at2; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000018439; 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; 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; 1.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00523,
KW ECO:0000313|EMBL:EGJ70970.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000018439};
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 22..90
FT /note="UDP-3-O-[3-hydroxymyristoyl] glucosamine N-
FT acyltransferase non-repeat region"
FT /evidence="ECO:0000259|Pfam:PF04613"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00523"
SQ SEQUENCE 345 AA; 36749 MW; 6566C02BBA346545 CRC64;
MEFSAKQIAS YIQGEIIGDE NATVHTFAKI EEGVSGAISF LSNPKYTHYI YNTQSSIVLV
NKDFKPEKPI SATLIKVDNA YDSLAKLLTL YEASKPKKTG IDSLASIAHT AKIGKNVYIA
PYVVIGENAV VGDNSAIYPH TYVGDNAKIG ANTTLYSNVN IYHECIIGNN CILHSGVVVG
ADGFGFAPTA EGYEKIPQIG IAIIEDNVEI GANTCIDRAT MGATIIRKGV KLDNLIQIAH
NDEVGSHTVI AAQAGVAGST KIGQWCMIGG QAGLAGHAKI GDKVGIAAQS GIPGNIKSGN
QVMGSPAFEA RQYFKAASVF KKLPDIYMEI NMLRKELNEI KGKLK
//
