ID   A0A8J5ISS3_9STRA        Unreviewed;       580 AA.
AC   A0A8J5ISS3;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   27-NOV-2024, entry version 7.
DE   RecName: Full=Alkylglycerone-phosphate synthase {ECO:0000256|ARBA:ARBA00012385, ECO:0000256|RuleBase:RU363113};
DE            Short=Alkyl-DHAP synthase {ECO:0000256|RuleBase:RU363113};
DE            EC=2.5.1.26 {ECO:0000256|ARBA:ARBA00012385, ECO:0000256|RuleBase:RU363113};
GN   ORFNames=JG688_00007113 {ECO:0000313|EMBL:KAG6965624.1};
OS   Phytophthora aleatoria.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=2496075 {ECO:0000313|EMBL:KAG6965624.1, ECO:0000313|Proteomes:UP000709295};
RN   [1] {ECO:0000313|EMBL:KAG6965624.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZFS 4037 {ECO:0000313|EMBL:KAG6965624.1};
RA   Mcdougal R., Panda P., Williams N., Studholme D.J.;
RT   "Phytophthora aleatoria, a newly-described species from Pinus radiata is
RT   distinct from Phytophthora cactorum isolates based on comparative
RT   genomics.";
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the exchange of an acyl for a long-chain alkyl
CC       group and the formation of the ether bond in the biosynthesis of ether
CC       phospholipids. {ECO:0000256|RuleBase:RU363113}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long chain fatty alcohol + a 1-acylglycerone 3-phosphate = a
CC         1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+);
CC         Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26;
CC         Evidence={ECO:0000256|RuleBase:RU363113};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR625650-3,
CC         ECO:0000256|RuleBase:RU363113};
CC   -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004670, ECO:0000256|RuleBase:RU363113}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU363113}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|RuleBase:RU363113}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|RuleBase:RU363113}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG6965624.1}.
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DR   EMBL; JAENGY010000331; KAG6965624.1; -; Genomic_DNA.
DR   Proteomes; UP000709295; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR46568; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR46568:SF1; ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE, PEROXISOMAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR625650-3, ECO:0000256|RuleBase:RU363113};
KW   Flavoprotein {ECO:0000256|RuleBase:RU363113};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU363113};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU363113};
KW   Peroxisome {ECO:0000256|RuleBase:RU363113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000709295};
KW   Transferase {ECO:0000256|RuleBase:RU363113}.
FT   DOMAIN          142..291
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   ACT_SITE        488
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT   BINDING         210..216
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         223..226
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT   BINDING         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT   SITE            326
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ   SEQUENCE   580 AA;  63838 MW;  5963279CCA7E1D12 CRC64;
     MSDTTPSVAR MRAILRQISA GGQPASVSPP STPSPPLALS PATRWNGWGF QDTKLFVNSN
     KVIEISGARY AEVFANAPNR TLPSLLPWAE KRLGLDADRR SAPSITCPEE LRLKNQLDEG
     GETYKRLNQF LHLASEELDI KTSTTIEERV RHGHGQTCED VFRLRHVRDV ERVPDAVVEN
     MIAVVEAGIT GLDLHERLRH RGLTLGHEPD SWEFSTLGGW IATRASGMKK NTYGNIEDLV
     VNITTVTPQG TMQRAANVPR AAMGPDMNNA MMGSEGIFGV HTLVTLRLRE FPTVQVYDSL
     IFPSLEHGVA ALKEITRAGC EPASLRLLDN TQFQLGQALK TSSTTNKFTA GVIDFAKKTY
     VTKIRGFDVN EMCAATVLLE GASHQKVAEQ QKSIQTIAKR HEGMVGGEEN GKRGYFFTYI
     IAYLRDFALD YYFMSESFEA SVPWTNARQL ITDIKLAINS VAAKRDVKIP PLIACRISQV
     YDTGVCVYVY YGINYFGVNE PMTLFRETEL AAVDAIVRNG GALSHHHGVG KHRLAWLPAA
     VSPPAIAAIQ GIKSALDPTN VFAVTNLQPS KNHVESKHEA
//