ID A0A091N8D8_9PASS Unreviewed; 657 AA.
AC A0A091N8D8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dihydroxyacetone phosphate acyltransferase {ECO:0000256|ARBA:ARBA00044178};
DE EC=2.3.1.42 {ECO:0000256|ARBA:ARBA00044061};
DE AltName: Full=Glycerone-phosphate O-acyltransferase {ECO:0000256|ARBA:ARBA00044290};
DE Flags: Fragment;
GN ORFNames=N310_10995 {ECO:0000313|EMBL:KFP85277.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85277.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP85277.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85277.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the
CC first step in the biosynthesis of plasmalogens, a subset of
CC phospholipids that differ from other glycerolipids by having an alkyl
CC chain attached through a vinyl ether linkage at the sn-1 position of
CC the glycerol backbone, and which unique physical properties have an
CC impact on various aspects of cell signaling and membrane biology.
CC {ECO:0000256|ARBA:ARBA00043888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone
CC 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00043791};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17658;
CC Evidence={ECO:0000256|ARBA:ARBA00043791};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + hexadecanoyl-CoA = 1-
CC hexadecanoylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:40715,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:58303; Evidence={ECO:0000256|ARBA:ARBA00043732};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40716;
CC Evidence={ECO:0000256|ARBA:ARBA00043732};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00037925}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SUBUNIT: Part of a heterotrimeric complex composed of GNPAT, AGPS and a
CC modified form of GNPAT. {ECO:0000256|ARBA:ARBA00044003}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00043943}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00043943}; Matrix side
CC {ECO:0000256|ARBA:ARBA00043943}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; KK843202; KFP85277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N8D8; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:InterPro.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR028353; DHAPAT.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500063; DHAPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:KFP85277.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFP85277.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..261
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP85277.1"
FT NON_TER 657
FT /evidence="ECO:0000313|EMBL:KFP85277.1"
SQ SEQUENCE 657 AA; 74816 MW; D3FC420CCA4F119A CRC64;
QKELTSKKRD EFEDILEERR LSSDLRYAMK CYSPVIYKGL SPCKPSAIKS AVLQSEQVQY
VIKQLAKELG ESPDIIQEEA MEILDEMGHS MQLGAVRFFA FTLSKIFKQL FQRVCVNEEG
MQRLQHAIQE HPVVLLPSHR SYVDFLMLSY LLYTYDLALP VIAAGIFLGM KIVGELLRRA
GAFFMRRSFG GNRLYWAVFA EYVKTMLRSG YAPIEFFLEG TRSRTAKTLT PKFGLLSIVM
EPFFKREVFD TYLVPISISY ERILEESLYA YELLGVPKPK ESTSGLLKAR RILSDNFGTI
HIYVGQPVSL RTLASGRINR CPYNLVPRHL PQKPSEDIQE FVSDVAYKME LLQIENMVLS
PWVLVAAVLL QNLPAVEFEL LIEKTLWLKG LTQTFGGFIE WPDNLCAKKA VLSGLTLHSN
IARLVDGHVV LNDKGAEEGA IGEMVFKRAL SILMCATYRN QLLNVFVRPS LVAVALQMTH
SFRKEEVYSC FTFLRDVFVD EFIFFPGISL KDFEEGCFLL TKCDAIQMSQ QEIYPTDKGN
VTVSFLSAMF RPFVEGYQLI FRYLSKEIKE AFTEKQFIPG VRNFVFQLLE KGTTQCYEAL
SSDMQKNALA ALVQLGAVMK KKMSNGFTYS VNQEAVSKIL DVFDARMPVQ KPVAARL
//
