LPXH_SHEFN
ID LPXH_SHEFN Reviewed; 241 AA.
AC Q07ZX3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sfri_2601;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000447; ABI72442.1; -; Genomic_DNA.
DR RefSeq; WP_011638051.1; NC_008345.1.
DR AlphaFoldDB; Q07ZX3; -.
DR SMR; Q07ZX3; -.
DR STRING; 318167.Sfri_2601; -.
DR EnsemblBacteria; ABI72442; ABI72442; Sfri_2601.
DR KEGG; sfr:Sfri_2601; -.
DR eggNOG; COG2908; Bacteria.
DR HOGENOM; CLU_074586_0_0_6; -.
DR OMA; FDFWFEY; -.
DR OrthoDB; 1690667at2; -.
DR UniPathway; UPA00359; UER00480.
DR Proteomes; UP000000684; 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; IPR004843; Calcineurin-like_PHP_ApaH.
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; PF00149; Metallophos; 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..241
FT /note="UDP-2,3-diacylglucosamine hydrolase"
FT /id="PRO_1000025083"
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 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 42
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 42
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 79..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00575"
SQ SEQUENCE 241 AA; 27367 MW; F6235E7F2544E9D1 CRC64;
MKKTIFVGDL HLSADRPDIT QAFIYFLNHG LDNTEALYII GDLFEVWMGD DIAESFTIAI
AEAIKTVSNS IPVYFTHGNR DFMVDKQFCL RAGMKILPEV YCINLYGVNT VILHGDSLCT
LDIAYQRFRR FRSLDIVRWV YSHLPKKTRL NIAAKIRQKS VQGNQQKHYE IMDVESSAVT
ALLASTGCQR MIHGHTHRPA IHQLTAQEQR VVVGDWYTQG SVLNVSEKGC ELVTLPFSET
N
