(data stored in ACNUC7421 zone)

SWISSPROT: LPXH_ECOL5

ID   LPXH_ECOL5              Reviewed;         240 AA.
AC   Q0TKB7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, 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=ECP_0585;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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(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}.
DR   EMBL; CP000247; ABG68614.1; -; Genomic_DNA.
DR   RefSeq; WP_000212245.1; NC_008253.1.
DR   SMR; Q0TKB7; -.
DR   EnsemblBacteria; ABG68614; ABG68614; ECP_0585.
DR   KEGG; ecp:ECP_0585; -.
DR   eggNOG; ENOG4105F10; Bacteria.
DR   eggNOG; COG2908; LUCA.
DR   HOGENOM; HOG000261930; -.
DR   KO; K03269; -.
DR   OMA; FDFWFEY; -.
DR   BioCyc; ECOL362663:G1G5S-611-MONOMER; -.
DR   UniPathway; UPA00359; UER00480.
DR   Proteomes; UP000009182; 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   HAMAP; MF_00575; LpxH; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase.
DR   PANTHER; PTHR34990:SF1; PTHR34990:SF1; 1.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   TIGRFAMs; TIGR01854; lipid_A_lpxH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0TKB7.
DR   SWISS-2DPAGE; Q0TKB7.
KW   Cell inner membrane; Cell membrane; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Membrane; Metal-binding.
FT   CHAIN           1..240
FT                   /note="UDP-2,3-diacylglucosamine hydrolase"
FT                   /id="PRO_1000025051"
FT   REGION          79..80
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           8
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           10
FT                   /note="Manganese 1; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           41
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           41
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           79
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           114
FT                   /note="Manganese 2; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           195
FT                   /note="Manganese 2; via pros nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   METAL           197
FT                   /note="Manganese 1; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         122
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         160
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         164
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         167
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT   BINDING         195
FT                   /note="Substrate; via tele nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
SQ   SEQUENCE   240 AA;  26879 MW;  3F3EB8F18BADB274 CRC64;
     MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD DPNPLHHQMA
     AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE KVLELYGRRV LIMHGDTLCT
     DDAGYQAFRA KVHKPWLQTL FLALPLFVRK RIAARMRANS KEANSSKSLA IMDVNQNAVV
     SAMEKHQVQW LIHGHTHRPA VHELIANQQT AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
//

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