(data stored in ACNUC10821 zone)

SWISSPROT: C8U2K5_ECO10

ID   C8U2K5_ECO10            Unreviewed;       240 AA.
AC   C8U2K5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 69.
DE   RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000256|HAMAP-Rule:MF_00575, ECO:0000256|SAAS:SAAS00911804};
DE            EC=3.6.1.54 {ECO:0000256|HAMAP-Rule:MF_00575, ECO:0000256|SAAS:SAAS00911805};
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:BAI29363.1};
GN   OrderedLocusNames=ECO103_0496 {ECO:0000313|EMBL:BAI29363.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29363.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29363.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|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:0000256|HAMAP-Rule:MF_00575,
CC         ECO:0000256|SAAS:SAAS01122650};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         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
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 4/6. {ECO:0000256|HAMAP-
CC       Rule:MF_00575, ECO:0000256|SAAS:SAAS00911810}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00575, ECO:0000256|SAAS:SAAS00911815}; Peripheral membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_00575,
CC       ECO:0000256|SAAS:SAAS00911815}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_00575, ECO:0000256|SAAS:SAAS00911815}.
CC       Cytoplasm {ECO:0000256|SAAS:SAAS00911808}.
CC   -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00575, ECO:0000256|SAAS:SAAS00911803}.
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DR   EMBL; AP010958; BAI29363.1; -; Genomic_DNA.
DR   RefSeq; WP_000212264.1; NC_013353.1.
DR   EnsemblBacteria; BAI29363; BAI29363; ECO103_0496.
DR   KEGG; eoh:ECO103_0496; -.
DR   HOGENOM; HOG000261930; -.
DR   KO; K03269; -.
DR   OMA; FDFWFEY; -.
DR   BioCyc; ECOL585395:ECO103_RS02590-MONOMER; -.
DR   UniPathway; UPA00359; UER00480.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; C8U2K5.
DR   SWISS-2DPAGE; C8U2K5.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911809};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911818};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911813};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911800};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911812};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911817};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911807};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911806};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00575,
KW   ECO:0000256|SAAS:SAAS00911816}.
FT   DOMAIN        1    203       Metallophos_2. {ECO:0000259|Pfam:
FT                                PF12850}.
FT   REGION       79     80       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00575}.
FT   METAL         8      8       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   METAL        10     10       Manganese 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00575}.
FT   METAL        41     41       Manganese 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   METAL        41     41       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   METAL        79     79       Manganese 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   METAL       114    114       Manganese 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00575}.
FT   METAL       195    195       Manganese 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00575}.
FT   METAL       197    197       Manganese 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00575}.
FT   BINDING     122    122       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   BINDING     160    160       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   BINDING     167    167       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00575}.
FT   BINDING     195    195       Substrate; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00575}.
SQ   SEQUENCE   240 AA;  26938 MW;  BA77CF1426CA23F6 CRC64;
     MATLFIADLH LCVEEPAITA GFLRFLAGEA RKAEALYILG DLFEAWIGDD DPNPLHRQMA
     AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE KVLELYGRRV LIMHGDTLCT
     DDAGYQAFRA KVHKPWLQML FLALPLFVRK RIAARMRANS KEANSSKSLA IMDVNQNAVV
     SAMEKHQVQW LIHGHTHRPA VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
//

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