ADAS_CAEEL
ID ADAS_CAEEL Reviewed; 597 AA.
AC O45218;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26;
DE AltName: Full=Alkylglycerone-phosphate synthase;
GN Name=ads-1; ORFNames=Y50D7A.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9446784; DOI=10.1006/bbrc.1997.7950;
RA de Vet E.C.J.M., Prinsen H.C.M.T., van den Bosch H.;
RT "Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans
RT homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: evolutionary
RT switching of peroxisomal targeting signals.";
RL Biochem. Biophys. Res. Commun. 242:277-281(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; AJ002686; CAA05690.1; -; mRNA.
DR EMBL; FO081772; CCD73794.1; -; Genomic_DNA.
DR PIR; JC5829; JC5829.
DR RefSeq; NP_497185.1; NM_064784.7.
DR AlphaFoldDB; O45218; -.
DR SMR; O45218; -.
DR BioGRID; 40467; 2.
DR STRING; 6239.Y50D7A.7; -.
DR EPD; O45218; -.
DR PaxDb; O45218; -.
DR PeptideAtlas; O45218; -.
DR EnsemblMetazoa; Y50D7A.7.1; Y50D7A.7.1; WBGene00000081.
DR GeneID; 175192; -.
DR KEGG; cel:CELE_Y50D7A.7; -.
DR UCSC; Y50D7A.7.1; c. elegans.
DR CTD; 175192; -.
DR WormBase; Y50D7A.7; CE26144; WBGene00000081; ads-1.
DR eggNOG; KOG1233; Eukaryota.
DR GeneTree; ENSGT00940000156112; -.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; O45218; -.
DR OMA; PRCHDEV; -.
DR OrthoDB; 824020at2759; -.
DR PhylomeDB; O45218; -.
DR Reactome; R-CEL-75896; Plasmalogen biosynthesis.
DR UniPathway; UPA00781; -.
DR PRO; PR:O45218; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000081; Expressed in larva and 3 other tissues.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
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 GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
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 PANTHER; PTHR46568; PTHR46568; 1.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Peroxisome;
KW Reference proteome; Transferase.
FT CHAIN 1..597
FT /note="Alkyldihydroxyacetonephosphate synthase"
FT /id="PRO_0000128177"
FT DOMAIN 131..313
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 544..546
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOTIF 595..597
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 507
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 163..169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 232..238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 245..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 297..303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 348
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 597 AA; 66559 MW; 6224D6A11E0811AB CRC64;
MSASYQTIEH DVPQSYRDKI LKWNGWGYSD SQFAINKDGH VTFTGDKYEI SGKVMPHFRP
WFENYLGIDL GFVSPAQKLS DVIIDAPVEN EDIIEFLQEN KISFSNEARI RLMRGHGHTV
HDMINLREGK IPRLPDIVVW PKSEHEIVKI IEGAMSHNCA IIPIGGGTSV TNALDTPETE
KRAVISMDMA LLDKILWIDR ENLTCRAQAG IVGQSLERQL NKKGFTCGHE PDSIEFSTLG
GWVSTRASGM KKNKYGNIED LVVHLNFVCP KGIIQKQCQV PRMSSGPDIH QIILGSEGTL
GVVSEVTIKI FPIPEVKRFG SFVFPNFESG VNFFREVAIQ RCQPASLRLM DNDQFVMGQA
LKVASDSWWA DLKSSVSKMY ITSWKGFKVD EICAATCVYE GNREEVDQHE ERLNKLAEQF
HGVVGGAENG QYGYRLTFAI AYLRDLGMNH GVLGESFETS VPWDKVLSLC RNVKELMKRE
AKAQGVTHPV LANCRVTQVY DAGACVYFYF GFNARGLKNG LEVYDRIETA ARDEIIACGG
SISHHHGVGK IRKQWMLTTN GAVGIALLKA IKSELDPANI FASANLIDII GSPHCKL
