ID Q170V5_AEDAE Unreviewed; 595 AA.
AC Q170V5;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=AAEL007789 {ECO:0000313|EMBL:EAT40482.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT40482.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT40482.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40482.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT40482.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40482.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT40482.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT40482.1};
RG VectorBase;
RL Submitted (SEP-2012) 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 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 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|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU363113}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275,
CC ECO:0000256|RuleBase:RU363113}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000,
CC ECO:0000256|RuleBase:RU363113}.
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DR EMBL; CH477466; EAT40482.1; -; Genomic_DNA.
DR RefSeq; XP_001658665.1; XM_001658615.1.
DR AlphaFoldDB; Q170V5; -.
DR STRING; 7159.Q170V5; -.
DR PaxDb; 7159-AAEL007789-PA; -.
DR GeneID; 5569642; -.
DR KEGG; aag:5569642; -.
DR VEuPathDB; VectorBase:AAEL007789; -.
DR eggNOG; KOG1233; Eukaryota.
DR HOGENOM; CLU_017779_2_2_1; -.
DR OMA; MCHVSHA; -.
DR OrthoDB; 5474593at2759; -.
DR PhylomeDB; Q170V5; -.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000682892; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.300.330; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.3450; -; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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 SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 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|ARBA:ARBA00023140, ECO:0000256|RuleBase:RU363113};
KW Transferase {ECO:0000256|RuleBase:RU363113}.
FT DOMAIN 132..314
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 506
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 233..239
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 246..249
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 298..304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 349
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 595 AA; 66388 MW; DF727D38DC90FC78 CRC64;
MDSAVGGPEN VVPTIPKCRQ RLMRWDGWGY KDSRFEYDGK DCFFSGSRYP IGKGARLNRF
RDWVIDYFDV DTSKRLAAVE EPGVFPDPVR CVEFVDGLRN AGVEFSEDGM DRLMRCHGQT
LEDLGLLKNQ SYERLPDLVV WPRCHEDVVK IVTLAGEHDV ALMAVGGNSA VSGATTTPSV
HGRTVAVVDM TQMNRLLWLN KENLTACFEV GIVGQDLERT LKKQGFTLGH EPDSVEFSTL
GGWISTRASG MKKNSYGNIE DLVIRIKMVT GIGVLEKQFT APRVSCGPDF DQLVFGSEGT
LGIITEAVVR LRPVAPVSRC GSLVFPNFET GVHFLREVAK KRLQPASIRL LDNLQFQIGQ
YLQPDGPWHT ELVNGIKRQY LTTICGFKLD QIAAVTLVFE GDQKRVESHE KLIYTIAAKY
GALNAGSKNG EKGYVMTFVV AYIRDFGWDF NIMADSFETS VSWDKCLSLC ANVKSCVTKE
CERHGIRRLM ISYRVTQTYD DGCCVYFYMA LKHPDDHVNS VEVFKAIEDR ARDEILASGG
TLSHHHGVGK MRSKWYSACV SQVGVRVLKA IKRELDPKNI FAAGNLVDDG AISKL
//
