ADAS_DROME
ID ADAS_DROME Reviewed; 631 AA.
AC Q9V778;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26;
DE AltName: Full=Alkylglycerone-phosphate synthase;
GN Name=ADPS {ECO:0000312|FlyBase:FBgn0033983};
GN ORFNames=CG10253 {ECO:0000312|FlyBase:FBgn0033983};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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; AE013599; AAF58181.1; -; Genomic_DNA.
DR EMBL; AY094917; AAM11270.1; -; mRNA.
DR RefSeq; NP_001188935.1; NM_001202006.1.
DR RefSeq; NP_001188936.1; NM_001202007.2.
DR RefSeq; NP_001188937.1; NM_001202008.1.
DR RefSeq; NP_611006.1; NM_137162.3.
DR AlphaFoldDB; Q9V778; -.
DR SMR; Q9V778; -.
DR STRING; 7227.FBpp0292773; -.
DR PaxDb; Q9V778; -.
DR DNASU; 36669; -.
DR EnsemblMetazoa; FBtr0087428; FBpp0086558; FBgn0033983.
DR EnsemblMetazoa; FBtr0303760; FBpp0292772; FBgn0033983.
DR EnsemblMetazoa; FBtr0303761; FBpp0292773; FBgn0033983.
DR EnsemblMetazoa; FBtr0303762; FBpp0292774; FBgn0033983.
DR GeneID; 36669; -.
DR KEGG; dme:Dmel_CG10253; -.
DR UCSC; CG10253-RA; d. melanogaster.
DR CTD; 36669; -.
DR FlyBase; FBgn0033983; ADPS.
DR VEuPathDB; VectorBase:FBgn0033983; -.
DR eggNOG; KOG1233; Eukaryota.
DR GeneTree; ENSGT00940000156112; -.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; Q9V778; -.
DR OMA; PRCHDEV; -.
DR OrthoDB; 824020at2759; -.
DR PhylomeDB; Q9V778; -.
DR Reactome; R-DME-9033241; Peroxisomal protein import.
DR UniPathway; UPA00781; -.
DR BioGRID-ORCS; 36669; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36669; -.
DR PRO; PR:Q9V778; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033983; Expressed in crop (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q9V778; baseline and differential.
DR Genevisible; Q9V778; DM.
DR GO; GO:0005777; C:peroxisome; IDA:FlyBase.
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; ISS:FlyBase.
DR Gene3D; 1.10.45.10; -; 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; 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..631
FT /note="Alkyldihydroxyacetonephosphate synthase"
FT /id="PRO_0000128179"
FT DOMAIN 155..337
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..568
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOTIF 629..631
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 529
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 187..193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 256..262
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 321..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 372
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 631 AA; 70822 MW; AEDD6FDDA6BFB862 CRC64;
MAAKRNAVTT EAPESSAPGE GTALALDSRL SKRVESVIPK KRHEALKWFG WGYNDSQFYG
KDGIICFRGE KYPLGGCELP SFTKWVEKKF DLRVDTTKQY PQLPRTYPRP VENAPFLHEL
KGTTQVDYSA EGIDRLVRCH GQTLNDIYSL WHHKFRRIPD LVVWPRCHDE VVQLVRLANK
HNVMLVPFGG GTSVSGAITC PQNESRMICA LDTSQMNRLL WLNRENLTVC FESGIVGQDL
ERVLRSEGLT VGHEPDSYEF STLGGWVATR ASGMKKNVYG NIEDLVVRVR MVTPSGTLER
ECSAPRVSCG PDFNHVILGS EGTLGVITEV VLKVRPLPSL RRYGSLAFPN FEQGVLFMRE
VARRRCQPAS VRLMDNEQFM FGQALKPEKS WWASVVDAMK QRYVTSWKGI DLNQICAATL
LFEGDLKDVQ RQEALIYEIA EKFQGFPAGG QNGERGYILT FVIAYIRDFG LHQGIVAESF
ETSVPWDRCS LLCRSVKQRV VSECSKRSIN YYTISCRVTQ TYDAGACIYF YFGFRSTDVA
DPVELFEAIE HSARDEILSC GGSLSHHHGV GKIRSHWYRN AVTETGSSLY SAAKRHLDPK
NIFALGNLLP LEEAQASPPP PTSSTPPKAK L
