(data stored in ACNUC7421 zone)

SWISSPROT: LPXH_ECODH

ID   LPXH_ECODH              Reviewed;         240 AA.
AC   B1XGC2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 65.
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=ECDH10B_0480;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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: UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-
CC       alpha-D-glucosamine + H(2)O = 2-N,3-O-bis((3R)-3-
CC       hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate + UMP.
CC       {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; CP000948; ACB01649.1; -; Genomic_DNA.
DR   RefSeq; WP_000212247.1; NC_010473.1.
DR   ProteinModelPortal; B1XGC2; -.
DR   SMR; B1XGC2; -.
DR   EnsemblBacteria; ACB01649; ACB01649; ECDH10B_0480.
DR   KEGG; ecd:ECDH10B_0480; -.
DR   eggNOG; ENOG4105F10; Bacteria.
DR   eggNOG; COG2908; LUCA.
DR   HOGENOM; HOG000261930; -.
DR   KO; K03269; -.
DR   OMA; FDFWFEY; -.
DR   UniPathway; UPA00359; UER00480.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_00575; LpxH; 1.
DR   InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR010138; UDP-diacylglucosamine_Hdrlase.
DR   PANTHER; PTHR34990:SF3; PTHR34990:SF3; 1.
DR   Pfam; PF12850; Metallophos_2; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR01854; lipid_A_lpxH; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XGC2.
DR   SWISS-2DPAGE; B1XGC2.
KW   Cell inner membrane; Cell membrane; Hydrolase; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Membrane;
KW   Metal-binding.
FT   CHAIN         1    240       UDP-2,3-diacylglucosamine hydrolase.
FT                                /FTId=PRO_1000129521.
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;  26894 MW;  5004A2E471B7A7E9 CRC64;
     MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD DPNPLHRKMA
     AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE KVLELYGRRV LIMHGDTLCT
     DDAGYQAFRA KVHKPWLQTL FLALPLFVRK RIAARMRANS KEANSSKSLA IMDVNQNAVV
     SAMEKHQVQW LIHGHTHRPA VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
//

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