ID A0A0U1PWK2_9BURK Unreviewed; 268 AA.
AC A0A0U1PWK2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000256|HAMAP-Rule:MF_00575};
DE EC=3.6.1.54 {ECO:0000256|HAMAP-Rule:MF_00575};
DE AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000256|HAMAP-Rule:MF_00575};
GN Name=lpxH {ECO:0000256|HAMAP-Rule:MF_00575};
GN ORFNames=AAV94_13855 {ECO:0000313|EMBL:KKW66899.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW66899.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW66899.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW66899.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3-
CC diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X)
CC and UMP by catalyzing the attack of water at the alpha-P atom. Involved
CC in the biosynthesis of lipid A, a phosphorylated glycolipid that
CC anchors the lipopolysaccharide to the outer membrane of the cell.
CC {ECO:0000256|HAMAP-Rule:MF_00575}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC glucosaminyl 1-phosphate + 2 H(+) + UMP; Xref=Rhea:RHEA:25213,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:57957, ChEBI:CHEBI:78847; EC=3.6.1.54;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00575};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00575};
CC Note=Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
CC {ECO:0000256|HAMAP-Rule:MF_00575};
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 4/6. {ECO:0000256|HAMAP-
CC Rule:MF_00575}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00575}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00575}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00575}.
CC -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000256|HAMAP-
CC Rule:MF_00575}.
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:KKW66899.1}.
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DR EMBL; LBNQ01000041; KKW66899.1; -; Genomic_DNA.
DR RefSeq; WP_046742877.1; NZ_LBNQ01000041.1.
DR AlphaFoldDB; A0A0U1PWK2; -.
DR STRING; 1610491.AAV94_13855; -.
DR PATRIC; fig|1610491.3.peg.2940; -.
DR OrthoDB; 9783283at2; -.
DR UniPathway; UPA00359; UER00480.
DR Proteomes; UP000050580; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008758; F:UDP-2,3-diacylglucosamine hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07398; MPP_YbbF-LpxH; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR HAMAP; MF_00575; LpxH; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR043461; LpxH-like.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase.
DR NCBIfam; TIGR01854; lipid_A_lpxH; 1.
DR PANTHER; PTHR34990:SF1; UDP-2,3-DIACYLGLUCOSAMINE HYDROLASE; 1.
DR PANTHER; PTHR34990; UDP-2,3-DIACYLGLUCOSAMINE HYDROLASE-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00575};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00575};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00575};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00575}; Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT DOMAIN 20..219
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 25
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 27
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 215
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 217
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
SQ SEQUENCE 268 AA; 29303 MW; 1BA6AB73CC6AE156 CRC64;
MTFAELTVLP CGASSQPGVI DCLADLHLQR SQPRTWQAFR TYLEGTPASH ILLLGDLFEV
WVGDDCLQER GSFEAEVAQA LRDCTAGGKA VYFMHGNRDF VIGQDFAAAT GAQLLQDPTI
LRVQGAGAWL LSHGDALCTD DLPYQQFRAV SRNPAWQQKF LAQPLAARRA FAASIRHESQ
SRKQEQDAAS YVDLNADATR AWLHASGCST LIHGHTHMPA SHDLGDGLRR IVLSDWDLEA
RPARAEVLRL APAGTGDADW QRISLAST
//
