ID Q4FTV7_PSYA2 Unreviewed; 286 AA.
AC Q4FTV7;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=UDP-2,3-diacylglucosamine hydrolase {ECO:0000256|HAMAP-Rule:MF_00575};
DE EC=3.6.1.54 {ECO:0000256|HAMAP-Rule:MF_00575};
DE AltName: Full=UDP-2,3-diacylglucosamine diphosphatase {ECO:0000256|HAMAP-Rule:MF_00575};
GN Name=lpxH {ECO:0000256|HAMAP-Rule:MF_00575};
GN OrderedLocusNames=Psyc_0692 {ECO:0000313|EMBL:AAZ18551.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18551.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ18551.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_00575};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-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 IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 4/6. {ECO:0000256|HAMAP-
CC Rule:MF_00575}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00575}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00575}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00575}.
CC -!- SIMILARITY: Belongs to the LpxH family. {ECO:0000256|HAMAP-
CC Rule:MF_00575}.
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DR EMBL; CP000082; AAZ18551.1; -; Genomic_DNA.
DR RefSeq; WP_011279978.1; NC_007204.1.
DR AlphaFoldDB; Q4FTV7; -.
DR STRING; 259536.Psyc_0692; -.
DR KEGG; par:Psyc_0692; -.
DR eggNOG; COG2908; Bacteria.
DR HOGENOM; CLU_074586_0_0_6; -.
DR OrthoDB; 9783283at2; -.
DR UniPathway; UPA00359; UER00480.
DR Proteomes; UP000000546; 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 CDD; cd07398; MPP_YbbF-LpxH; 1.
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 NCBIfam; TIGR01854; lipid_A_lpxH; 1.
DR PANTHER; PTHR34990:SF1; UDP-2,3-DIACYLGLUCOSAMINE HYDROLASE; 1.
DR PANTHER; PTHR34990; UDP-2,3-DIACYLGLUCOSAMINE HYDROLASE-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00575};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00575};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00575};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00575};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00575}; Reference proteome {ECO:0000313|Proteomes:UP000000546}.
FT DOMAIN 19..222
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 22
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 104..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00575"
SQ SEQUENCE 286 AA; 32658 MW; A0E598E21E7C68B2 CRC64;
MQSFNHLMTT HPHEVQQVLI SDLHLSPEEP ALVQAFLALL DDCLALPQLK RLFILGDWFE
VWIGDDAYLS LSKDERQTHW LTPLSVKLKK LRVAGCEILV MHGNRDFLLG QPFCNLFGGE
LIYEPYTLTV GQKNYRLEHG DALCIDDKKY QFFRKVMRNR LTQWYLLSKS LEKRLAIADN
MRQKSQQNNA NKAAYIMDVN ENAVIQAITA SDALVHGHTH RPDIHPTSND KIRYVLGDWR
LLDSGTRQPK VSAVIGAVTA DDCLNKDKKP NNNGAEFGLF EFNITI
//
