LYPGN_MYCTO
ID LYPGN_MYCTO Reviewed; 261 AA.
AC P9WG50; L0T858; P64837; P71669;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Lysoplasmalogenase {ECO:0000250|UniProtKB:P9WG51};
DE EC=3.3.2.2 {ECO:0000250|UniProtKB:P9WG51};
GN OrderedLocusNames=MT1445;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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. {ECO:0000250|UniProtKB:P9WG51}.
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:0000250|UniProtKB:P9WG51};
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:0000250|UniProtKB:P9WG51};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WG51};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TMEM86 family. {ECO:0000305}.
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; AE000516; AAK45710.1; -; Genomic_DNA.
DR PIR; F70900; F70900.
DR AlphaFoldDB; P9WG50; -.
DR EnsemblBacteria; AAK45710; AAK45710; MT1445.
DR KEGG; mtc:MT1445; -.
DR HOGENOM; CLU_079086_3_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR012506; YhhN.
DR PANTHER; PTHR31885; PTHR31885; 1.
DR Pfam; PF07947; YhhN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Lipid metabolism; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..261
FT /note="Lysoplasmalogenase"
FT /id="PRO_0000428423"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 261 AA; 27391 MW; DFA3084579718A91 CRC64;
MGSIAGFSSA VLSKLGIPVP YAPRLLAGGW VVAGWAGLAY GVYLTVIALR LPPGSELTGH
AMLQPAFKAS MAVLLAAAAV AHPIGRERRW LVPALLLSAT GDWLLAIPWW TWAFVFGLGA
FLLAHLCFIG ALLPLARQAA PSRGRVAAVV AMCVASAGLL VWFWPHLGKD NLTIPVTVYI
VALSAMVCTA LLARLPTIWT AVGAVCFAAS DSMIGIGRFI LGNEALAVPI WWSYAAAEIL
ITAGFFFGRE VPDNAAAPTD S