(data stored in ACNUC7421 zone)

SWISSPROT: LPXH_ECO27

ID   LPXH_ECO27              Reviewed;         240 AA.
AC   B7UKK1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=E2348C_0457;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3-
CC       diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate
CC       (lipid X) and UMP by catalyzing the attack of water at the alpha-P
CC       atom. Involved in the biosynthesis of lipid A, a phosphorylated
CC       glycolipid that anchors the lipopolysaccharide to the outer
CC       membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00575}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-
CC         D-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
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-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-
CC       Rule:MF_00575}.
CC   -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00575}.
DR   EMBL; FM180568; CAS08005.1; -; Genomic_DNA.
DR   RefSeq; WP_000212243.1; NC_011601.1.
DR   SMR; B7UKK1; -.
DR   EnsemblBacteria; CAS08005; CAS08005; E2348C_0457.
DR   KEGG; ecg:E2348C_0457; -.
DR   KO; K03269; -.
DR   OMA; FDFWFEY; -.
DR   BioCyc; ECOL574521:E2348C_RS02395-MONOMER; -.
DR   UniPathway; UPA00359; UER00480.
DR   Proteomes; UP000008205; 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; B7UKK1.
DR   SWISS-2DPAGE; B7UKK1.
KW   Cell inner membrane; Cell membrane; Complete proteome; Hydrolase;
KW   Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism; Manganese;
KW   Membrane; Metal-binding.
FT   CHAIN         1    240       UDP-2,3-diacylglucosamine hydrolase.
FT                                /FTId=PRO_1000191028.
FT   REGION       79     80       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL         8      8       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL        10     10       Manganese 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00575}.
FT   METAL        41     41       Manganese 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL        41     41       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL        79     79       Manganese 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL       114    114       Manganese 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00575}.
FT   METAL       195    195       Manganese 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00575}.
FT   METAL       197    197       Manganese 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00575}.
FT   BINDING     122    122       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   BINDING     160    160       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   BINDING     164    164       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   BINDING     167    167       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00575}.
FT   BINDING     195    195       Substrate; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00575}.
SQ   SEQUENCE   240 AA;  26902 MW;  55FEB8EC96ADAB29 CRC64;
     MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD DPNPLHHQMA
     AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE KVLELYGRRV LIMHGDTLCT
     DDAGYQAFRA KVHKPWLQTL FLALPLFVRK RIAARMRANS KEANSSKSLA IMDVNQNAVV
     NAMEKHQVQW LIHGHTHRPA VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
//

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