ID A0A091XPX8_OPIHO Unreviewed; 362 AA.
AC A0A091XPX8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Neutral cholesterol ester hydrolase 1 {ECO:0000256|ARBA:ARBA00044162};
DE EC=3.1.1.71 {ECO:0000256|ARBA:ARBA00044060};
DE AltName: Full=Acetylalkylglycerol acetylhydrolase {ECO:0000256|ARBA:ARBA00044219};
DE AltName: Full=Arylacetamide deacetylase-like 1 {ECO:0000256|ARBA:ARBA00044256};
DE Flags: Fragment;
GN ORFNames=N306_05017 {ECO:0000313|EMBL:KFR15046.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR15046.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR15046.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR15046.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-
CC glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115,
CC ChEBI:CHEBI:75936; Evidence={ECO:0000256|ARBA:ARBA00023406};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564;
CC Evidence={ECO:0000256|ARBA:ARBA00023406};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycerol + H2O = 1-O-alkyl-sn-glycerol
CC + acetate + H(+); Xref=Rhea:RHEA:11552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:16291,
CC ChEBI:CHEBI:30089; EC=3.1.1.71;
CC Evidence={ECO:0000256|ARBA:ARBA00043796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11553;
CC Evidence={ECO:0000256|ARBA:ARBA00043796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester + H2O = a fatty acid + cholesterol + H(+);
CC Xref=Rhea:RHEA:36403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043699};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404;
CC Evidence={ECO:0000256|ARBA:ARBA00043699};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000256|ARBA:ARBA00023350};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000256|ARBA:ARBA00023350};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}. Microsome
CC {ECO:0000256|ARBA:ARBA00004144}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00010515}.
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DR EMBL; KK735627; KFR15046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091XPX8; -.
DR STRING; 30419.A0A091XPX8; -.
DR ESTHER; opiho-a0a091xpx8; Arylacetamide_deacetylase.
DR PhylomeDB; A0A091XPX8; -.
DR Proteomes; UP000053605; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR017157; Arylacetamide_deacetylase.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF33; SIMILAR TO HYPOTHETICAL PROTEIN C130079G13; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:KFR15046.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 63..221
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 275..335
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 302
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR15046.1"
FT NON_TER 362
FT /evidence="ECO:0000313|EMBL:KFR15046.1"
SQ SEQUENCE 362 AA; 40969 MW; 8E0869F871AA1150 CRC64;
CHLIHYLRLS HHLIALNYVI CTFDKLKSVS PEDINITDAV FDGVEVRVFE PPAKQDERLK
RSVVYIHGGG WALASARTSL YNNLCRIMAE SLSAVVVSVE YRLVPEVCFP EQFHDALRAT
KHFLQPDVLA EYSVDPSRIA ISGDSAGGNL AAAVCQQLSK DEHLTIRPKL QALIYPVLQA
FDFNTPSYQQ NMNMPVLPRY VMINYWIDYF NGNYDLAHSL LINNHTALDV GQALSFRGRL
NWTSLLPSSF KKNYKPVIQT TGKADIVEEI PALLDVRAVP LLAENETLQL QPKTYILTCE
NDVLRDDGVM YAKRLENAGV EVTLDHFDDC FHGCMIFTIW PTDFSAGVQT RNSYIKWLDE
NL
//
