LPXH_KLEP7
ID LPXH_KLEP7 Reviewed; 240 AA.
AC A6T5R0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000255|HAMAP-Rule:MF_00575};
DE EC=3.6.1.54 {ECO:0000255|HAMAP-Rule:MF_00575};
DE AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000255|HAMAP-Rule:MF_00575};
GN Name=lpxH {ECO:0000255|HAMAP-Rule:MF_00575};
GN OrderedLocusNames=KPN78578_04700; ORFNames=KPN_00480;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_00575};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00575};
CC Note=Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00575}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00575}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00575}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00575}.
CC -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000255|HAMAP-
CC Rule:MF_00575}.
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DR EMBL; CP000647; ABR75931.1; -; Genomic_DNA.
DR RefSeq; WP_004191610.1; NC_009648.1.
DR PDB; 6PH9; X-ray; 1.92 A; A=2-240.
DR PDB; 6PIB; X-ray; 2.26 A; A=2-240.
DR PDB; 6PJ3; X-ray; 2.25 A; A=1-240.
DR PDB; 6WII; X-ray; 1.85 A; A=1-240.
DR PDBsum; 6PH9; -.
DR PDBsum; 6PIB; -.
DR PDBsum; 6PJ3; -.
DR PDBsum; 6WII; -.
DR AlphaFoldDB; A6T5R0; -.
DR SMR; A6T5R0; -.
DR STRING; 272620.KPN_00480; -.
DR DNASU; 5341259; -.
DR EnsemblBacteria; ABR75931; ABR75931; KPN_00480.
DR KEGG; kpn:KPN_00480; -.
DR HOGENOM; CLU_074586_0_0_6; -.
DR OMA; FDFWFEY; -.
DR UniPathway; UPA00359; UER00480.
DR Proteomes; UP000000265; Chromosome.
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 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 PANTHER; PTHR34990; PTHR34990; 1.
DR PANTHER; PTHR34990:SF1; PTHR34990:SF1; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR01854; lipid_A_lpxH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism; Manganese;
KW Membrane; Metal-binding; Reference proteome.
FT CHAIN 1..240
FT /note="UDP-2,3-diacylglucosamine hydrolase"
FT /id="PRO_1000025060"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 79..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:6WII"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6PIB"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6PH9"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6WII"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6WII"
SQ SEQUENCE 240 AA; 27087 MW; 64D42BB7EB0CF13E CRC64;
MATLFIADLH LQTEEPAITA GFLRFLQGEA RQADALYILG DLFEAWIGDD DPNPLHQQIA
SAIKAVVDAG VPCYFIHGNR DFLVGQRFAR QSGMILLAEE ERLDLYGREV LIMHGDTLCT
DDQGYLAFRA KVHTPWIQRL FLALPLFIRH RIAARMRADS KAANSSKSME IMDVNPQAVV
DAMERHHVQW LIHGHTHRPA VHELQANGQP AWRVVLGAWH SEGSMVKVTP DDVELIHFPF
