ID A0A158Q9N8_ENTVE Unreviewed; 589 AA.
AC A0A158Q9N8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=EVEC_LOCUS2355 {ECO:0000313|EMBL:VDD87212.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000264701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000264701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD87212.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) 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|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|ARBA:ARBA00008000,
CC ECO:0000256|RuleBase:RU363113}.
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DR EMBL; UXUI01007365; VDD87212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158Q9N8; -.
DR STRING; 51028.A0A158Q9N8; -.
DR WBParaSite; EVEC_0000264701-mRNA-1; EVEC_0000264701-mRNA-1; EVEC_0000264701.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; 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; 3.30.160.650; -; 1.
DR Gene3D; 3.30.300.330; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.3450; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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|RuleBase:RU363113};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131};
KW Transferase {ECO:0000256|RuleBase:RU363113}.
FT DOMAIN 130..312
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 502
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 162..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 231..237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 244..247
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 296..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 347
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 589 AA; 65592 MW; 1E1933A4DDD4C1EA CRC64;
MVPSYACDCN LSILFRDSAL KWNGWGFTDS SFQINNKGQV TFTGQRYNMS GEVMPFFRPW
FEKNLGVDLD HRTPSQLRSD LVVPPAVVNQ PFINFLKANN IGYSNAPQHR VVRSHGHTVH
EIWKLRHGKF ERLVDIVAWP KNESEIIKIV SAANEFNVVI IPIGGGTSVS HALECPSDER
RSICSVDLAL MDKILWVDEA NLLCRAEAGI IGLKLEKELN AKGFTCGHEP DSIELSTLGG
WISTRASGMK KNKYGNIEDL LVHVSMVSSK GVVRKYCQVP RISGGPDLHQ IILGSEGILG
VISEATVKIF PLPEVKKFGS LVFPSFENGV NFMREVARQR CQPASLRLVD NEQFVMGQSL
KIQRNLWDTL ASNLSKLYIT KWKGFKMVAA TICYEGSGQE VELQERTLNS IAEAFKGVAG
GEESGKYGYM LTFAIAYLRD MGMELSVLGE SFETSVPWNK TLLLCRNVKE LIKREAKANG
VRYPVLSTCR VTQVYDSGAC VYFYFGFNYR GVKDPLEVYD KIEAAARDEI IACGGCISHH
HGVGKLRRPW MAVTVGEAGI SVIKAIKEEL DPKNIFACGN LIDMKKSKL
//
