ID A0A091LN89_CARIC Unreviewed; 666 AA.
AC A0A091LN89;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=N322_06840 {ECO:0000313|EMBL:KFP60651.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP60651.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP60651.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP60651.1};
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; KK503872; KFP60651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LN89; -.
DR Proteomes; UP000054116; 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:KFP60651.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFP60651.1}.
FT DOMAIN 138..270
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP60651.1"
FT NON_TER 666
FT /evidence="ECO:0000313|EMBL:KFP60651.1"
SQ SEQUENCE 666 AA; 75767 MW; 7AAA28AB481C6FE6 CRC64;
FVCSQQKELT SKKRDEFEDI LEERRLSSDL RYAMKCYTPV IYKGLSPCKP NAIKSAVLQS
EQVQYVIKQL AKEMGESPDI IQEEAMEILD EMGHSMQLGA VRFFAFTLSK IFKQLFQRVC
VNEEGMQRLQ HAIQEHPVVL LPSHRSYVDF LMLSYLLYTY DLALPVIAAG IGKADFLGMK
IVGELLRRAG AFFMRRSFGG NRLYWAVFAE YVKTMLRTGY APIEFFLEGT RSRTAKTLTP
KFGLLSIVME PFFKREVFDT YLVPISISYE RILEESLYAY ELLGVPKPKE STSGLLKARR
ILSDSFGTIH IYVGQPVSLR TLASGRINRC PYNLVPRHLP QKPSEDIQEF VSDVAYKMEL
LQIENMVLSP WVLVAAVLLQ NLPAMDFELL IEKTLWLKGL TQTFGGFIEW PDNLCAKKAV
LSGLSLHSNI ARLVDGRVVL NDKGGEDGAI GEIVFKRALA ILMCATYRNQ LLNVFVRPSL
VALALQMTRS FRKEEVYSCF SFLRDVFSDE FIFFPGISLK DFEEGCFLLI KCDAIQTSQQ
EIYPTDKGSV TVSFLSAMFR PFVEGYQLIF RYLSKETKEA FTEKQFIPGV RNFVFQLLEK
GNTQCYEALS SDLQKNALAA LVQLGAVKKK KMANGFTFNV NQEAVNKILD MFDTRIPVQK
PVAARL
//
