ID U6LUM5_9EIME Unreviewed; 642 AA.
AC U6LUM5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
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=EBH_0072280 {ECO:0000313|EMBL:CDJ54037.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ54037.1};
RN [1] {ECO:0000313|EMBL:CDJ54037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ54037.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ54037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ54037.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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|RuleBase:RU363113}.
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DR EMBL; HG713545; CDJ54037.1; -; Genomic_DNA.
DR AlphaFoldDB; U6LUM5; -.
DR EnsemblProtists; CDJ54037; CDJ54037; EBH_0072280.
DR VEuPathDB; ToxoDB:EBH_0072280; -.
DR OrthoDB; 2898095at2759; -.
DR UniPathway; UPA00781; -.
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|RuleBase:RU363113};
KW Transferase {ECO:0000256|RuleBase:RU363113}.
FT DOMAIN 181..363
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 560
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 213..219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 282..288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 295..298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 347..353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 497
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-2"
FT SITE 398
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 642 AA; 70970 MW; 58CC502CBB4C4F5D CRC64;
MSSGGNDSRL SSSTGVTRRG NDQKVSAQQA IALQSPSSLR LPLRFPPDAF AALRLPAHEI
HHGRNRTAVC KTNGWGFKDT YIYFLDKTTL TVTGNRYPLC GQRLQHWQRF TKSIEGLDLE
AKSLPKEEII ISPQRLVKRE FLRDLLSRAP GVEVSEDGLE RLYHGHGHTC AEIFALRYGQ
IERLPDVVLF PKCHEDVEAI VACAVQHGVC LIPFGGGTSV TLGLAVPEDE QRMVATVSLS
YMQKILSLDR DALLLTVEAG AVGAVLEEQL RRLGVTVGHE PDSLEFSTVG GWVATRASGM
KKNAYGNIED LLIDAVVVTP QGTLNQRLAA PRVSSGPSVQ QLVLGSEGTL GIITQVVLKV
KVLPEEKIYG CLVFPNFEIG VAFMRHVALN KLQPASIRLM DKRQTQCGAL FRAVPPGGLG
LRDTLTDGIK NFYLNKIKGW REEDLCACTL LFEGSKEEVA SQQRNLYKAA KGFGGLPAGA
KNGQRGYQMT FLIAYVRDFI MDHFWVFESF EASIAWPLVL KCRNSVHNYI TKECKRLGIR
HPPLVMTRLT QVYDAGAVLY FYFGFNRAGI ENPMKVYKQI EDGARKVMMD LGGSISHHHG
IGKLRREFLP SAVGETSVAV LRGVKTCLDP KNIFGCRNLF DT
//
