LYPGN_LEGPH
ID LYPGN_LEGPH Reviewed; 216 AA.
AC Q5ZU17;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Lysoplasmalogenase {ECO:0000303|PubMed:25445671};
DE EC=3.3.2.2 {ECO:0000269|PubMed:25445671};
DE AltName: Full=LpYhhN {ECO:0000303|PubMed:25445671};
GN OrderedLocusNames=lpg1991 {ECO:0000312|EMBL:AAU28060.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=25445671; DOI=10.1016/j.bbamem.2014.11.011;
RA Jurkowitz M.S., Patel A., Wu L.C., Krautwater A., Pfeiffer D.R., Bell C.E.;
RT "The YhhN protein of Legionella pneumophila is a Lysoplasmalogenase.";
RL Biochim. Biophys. Acta 1848:742-751(2015).
RN [3]
RP ERRATUM OF PUBMED:25445671, AND ACTIVITY REGULATION.
RX PubMed=30463702; DOI=10.1016/j.bbamem.2018.09.001;
RA Jurkowitz M.S., Patel A., Wu L.C., Krautwater A., Pfeiffer D.R., Bell C.E.;
RL Biochim. Biophys. Acta 1861:344-344(2019).
CC -!- FUNCTION: Specifically hydrolyzes the vinyl ether bond of
CC lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to
CC release a fatty aldehyde and glycerophospho-choline or glycerophospho-
CC ethanolamine (PubMed:25445671). Has no activity on diradyl plasmalogen,
CC 1-alkenyl-glycerol, and monoacylglycerophospho-ethanolamine or
CC monoacylglycerophospho-choline (PubMed:25445671). May serve to protect
CC the bacterium from lysis by lysoplasmalogen derived from plasmalogens
CC of the host (PubMed:25445671). {ECO:0000269|PubMed:25445671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-
CC saturated aldehyde + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:22544, ChEBI:CHEBI:15377, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:73359, ChEBI:CHEBI:77287; EC=3.3.2.2;
CC Evidence={ECO:0000269|PubMed:25445671};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + H2O = a
CC 2,3-saturated aldehyde + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:16905, ChEBI:CHEBI:15377, ChEBI:CHEBI:73359,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:143890; EC=3.3.2.2;
CC Evidence={ECO:0000269|PubMed:25445671};
CC -!- ACTIVITY REGULATION: Competitively inhibited by lysophosphatidic acid.
CC {ECO:0000269|PubMed:30463702}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for lysoplasmenylcholine {ECO:0000269|PubMed:25445671};
CC KM=45 uM for lysoplasmenylethanolamine {ECO:0000269|PubMed:25445671};
CC Vmax=12 umol/min/mg enzyme with lysoplasmenylcholine as substrate
CC {ECO:0000269|PubMed:25445671};
CC Vmax=11 umol/min/mg enzyme with lysoplasmenylethanolamine as
CC substrate {ECO:0000269|PubMed:25445671};
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:25445671};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:25445671}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TMEM86 family. {ECO:0000305}.
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DR EMBL; AE017354; AAU28060.1; -; Genomic_DNA.
DR RefSeq; WP_010947707.1; NC_002942.5.
DR RefSeq; YP_096007.1; NC_002942.5.
DR STRING; 272624.lpg1991; -.
DR PaxDb; Q5ZU17; -.
DR DNASU; 3078628; -.
DR EnsemblBacteria; AAU28060; AAU28060; lpg1991.
DR GeneID; 66491122; -.
DR KEGG; lpn:lpg1991; -.
DR PATRIC; fig|272624.6.peg.2084; -.
DR eggNOG; COG3714; Bacteria.
DR HOGENOM; CLU_079086_0_0_6; -.
DR OMA; ACFKCLP; -.
DR BRENDA; 3.3.2.2; 2943.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR012506; YhhN.
DR PANTHER; PTHR31885; PTHR31885; 1.
DR Pfam; PF07947; YhhN; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..216
FT /note="Lysoplasmalogenase"
FT /id="PRO_0000456219"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 216 AA; 24536 MW; 9E737F88BAC2A4AF CRC64;
MTYSFSKPVS WVFLFTAVIY LVSLSFIQYP ATTVLKPIPI VCLIVGVFRT SLSSSAKILL
ILALVFSLAG DVVLTLPFSL QLELGIACFL LAHCFYITLF LKSFEFNRLH LFYYLPIFLF
MGFAAFTMIP YLGNLLIPVM IYFCVLMLMV FSAFQVKKET LTISSGALFF LISDLTLALN
LFIYTQADVR IFVMFTYYVA QFLLTFGLVR LYEKGG
