ID G7G7Z1_9GAMM Unreviewed; 245 AA.
AC G7G7Z1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:GAA81514.1};
GN ORFNames=P20495_4050 {ECO:0000313|EMBL:GAA81514.1};
OS Pseudoalteromonas sp. BSi20495.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA81514.1, ECO:0000313|Proteomes:UP000003050};
RN [1] {ECO:0000313|Proteomes:UP000003050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX PubMed=22275105; DOI=10.1128/JB.06427-11;
RA Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA Chen X.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT ice.";
RL J. Bacteriol. 194:908-909(2012).
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:GAA81514.1}.
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DR EMBL; BADY01000170; GAA81514.1; -; Genomic_DNA.
DR RefSeq; WP_008139050.1; NZ_BADY01000170.1.
DR AlphaFoldDB; G7G7Z1; -.
DR UniPathway; UPA00359; UER00480.
DR Proteomes; UP000003050; 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}.
FT DOMAIN 6..203
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 45
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 45
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 83
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
SQ SEQUENCE 245 AA; 28281 MW; 2EDEC0AE2878F0B6 CRC64;
MTRQTYFIAD LHLSENRPDI SAAFFDFLNT HILNKDVDAL YILGDFFEVW VGDDYITALS
ADVAKHLSAV NDGGTPVYFI HGNRDFIMRK QYADMAAMTL LDEQTVIDLY GTPTVILHGD
EMCTQDTEYQ NFRKKSRGWW WPKLMLAMPL WYRKKIARNA REKSKLSQVD KPIEILDVVD
EAVLATFAKH NVTNMIHGHT HRPNVHTYKV NEQTLTRTVL GDWYTQGSYF VVTPKSQELI
NTPFA
//
