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LPXH_PSEF5
ID   LPXH_PSEF5              Reviewed;         250 AA.
AC   Q4K9R8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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}; OrderedLocusNames=PFL_3915;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY93179.1; -; Genomic_DNA.
DR   RefSeq; WP_011062202.1; NC_004129.6.
DR   AlphaFoldDB; Q4K9R8; -.
DR   SMR; Q4K9R8; -.
DR   STRING; 220664.PFL_3915; -.
DR   EnsemblBacteria; AAY93179; AAY93179; PFL_3915.
DR   KEGG; pfl:PFL_3915; -.
DR   PATRIC; fig|220664.5.peg.4012; -.
DR   eggNOG; COG2908; Bacteria.
DR   HOGENOM; CLU_074586_0_0_6; -.
DR   OMA; FDFWFEY; -.
DR   OrthoDB; 1690667at2; -.
DR   UniPathway; UPA00359; UER00480.
DR   Proteomes; UP000008540; 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; IPR024654; Calcineurin-like_PHP_lpxH.
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; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR01854; lipid_A_lpxH; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Membrane; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..250
FT                   /note="UDP-2,3-diacylglucosamine hydrolase"
FT                   /id="PRO_1000025071"
FT   BINDING         7
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         40
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         40
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         78..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         194
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         196
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
SQ   SEQUENCE   250 AA;  28383 MW;  2BC4996A27D39969 CRC64;
     MILLISDLHL EEERPDITRA FLELLGGRAR AAEALYILGD FFEVWIGDDA MTPYQLSICQ
     ALRELSDSGT QIFLMHGNRD FMLGKAFCKA AGATLLKDPS VVDFYGEPVL LMHGDSLCTR
     DEAYMRMRRY LRNPLSLWIL RHLPLGTRRK LARKLRNESR AQTRMKANDI VDVTPDQVPQ
     VMQEHGVRTL VHGHTHRPAI HKLQIGEQAA KRIVLGDWDR QGWALQVDEQ GFQLAAFDFV
     PTQLALPGSP
 
 
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