ID   ADAS_TRYBB              Reviewed;         613 AA.
AC   O97157;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Alkyldihydroxyacetonephosphate synthase;
DE            Short=Alkyl-DHAP synthase;
DE            EC=2.5.1.26;
DE   AltName: Full=Alkylglycerone-phosphate synthase;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zomer A.M.W., Michels P.A.M., Opperdoes F.R.;
RT   "Molecular characterization of Trypanosoma brucei alkyl-
RT   dihydroxyacetonephosphate synthase.";
RL   Submitted (JAN-1999) 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:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol =
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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DR   EMBL; AF119091; AAD19697.1; -; Genomic_DNA.
DR   AlphaFoldDB; O97157; -.
DR   SMR; O97157; -.
DR   BRENDA; 2.5.1.26; 6519.
DR   UniPathway; UPA00781; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; ISS:UniProtKB.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Peroxisome;
KW   Transferase.
FT   CHAIN           1..613
FT                   /note="Alkyldihydroxyacetonephosphate synthase"
FT                   /id="PRO_0000128180"
FT   DOMAIN          126..307
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   REGION          534..536
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
FT   REGION          572..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           611..613
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        498
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..164
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..234
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         241..244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         291..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            342
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   613 AA;  69068 MW;  27BA9FBF2EB94E3A CRC64;
     MDKRMITDAF EEIKWNGWGD TGVCIKYDEA RQLPIHTNGK PMKHLLKFMK DDVLKVKGEF
     KIKPTPGLTK EEAIKRLPPP VVKQPFVDEL RQVLSKDQIR LDAYARLTHI FGKNYRDLWR
     VRRGMIDRPP DAVILPNNHD DCVKIMELAQ KHNVVVVPFG GGTNVTGGVE PNPFETRRMV
     ISIDMRRMGR MLHIDTESGT AVFEVGVLGP DIDEQLSRYG FMMGHDPDSY AYSTLGGWIA
     ARGSGAMSNK YGDIENMILA MRVVTPVGVV ETPLTSRPCG VDLNAMFVGS EGAFGLVTEA
     VVKIERLPEV KRYEGWLFPS FEVAFTAFHT CTRKGIHPCT MRLYDEDDTR LSFAASTDSG
     LVSTFFSKCF KKYIATVKGW NLSKISLVVV GFEGTKAQTN CQRSELVGVF QAFGATCLGT
     KPGNTWQEKK YDLPYLRDFA LAHNFWADVF ETSVLYTDAI HCWRAVKKSF AEVMAENGKN
     AWIGCHTAHQ YRFGCCLYFT FIGGQADEND LKIFLQVKKR AMEVMLQHRG NLTHHHGIGY
     EHVPWMKRYN GEGGLDAIMK FKKALDPKNI CNPGKLLPSP PSEKETPKAT QARQNREMMF
     DKMGIPGALQ AHL