ID A8XML6_CAEBR Unreviewed; 597 AA.
AC A8XML6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 Name=ads-1 {ECO:0000313|WormBase:CBG15716};
GN Synonyms=Cbr-ads-1 {ECO:0000313|EMBL:CAP33892.1};
GN ORFNames=CBG15716 {ECO:0000313|WormBase:CBG15716}, CBG_15716
GN {ECO:0000313|EMBL:CAP33892.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33892.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP33892.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP33892.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600979; CAP33892.1; -; Genomic_DNA.
DR RefSeq; XP_002640829.1; XM_002640783.1.
DR AlphaFoldDB; A8XML6; -.
DR STRING; 6238.A8XML6; -.
DR EnsemblMetazoa; CBG15716.1; CBG15716.1; WBGene00035862.
DR GeneID; 8582823; -.
DR KEGG; cbr:CBG_15716; -.
DR CTD; 8582823; -.
DR WormBase; CBG15716; CBP10094; WBGene00035862; Cbr-ads-1.
DR eggNOG; KOG1233; Eukaryota.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; A8XML6; -.
DR OMA; GTISHQH; -.
DR OrthoDB; 2898095at2759; -.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
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:UP000008549};
KW Transferase {ECO:0000256|RuleBase:RU363113}.
FT DOMAIN 131..313
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT ACT_SITE 507
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-1"
FT BINDING 163..169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 232..238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 245..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-3"
FT BINDING 297..303
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 348
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR625650-4"
SQ SEQUENCE 597 AA; 66634 MW; 693EBFF0A4DDABDF CRC64;
MSSAYQTLEH DVPQSYRDKI LKWNGWGYND SQFAINKDGH VTFTGDKYDI SGKVMPHFRP
WFENYLGIDL NYVSPAQKLS DVVIDAPVEN EDLIDFLKEN NISFSNSARI RLMRAHGHTV
HDMVNLREGK IPRLPDVVVW PKTEQEIVKI IEGAMSHNCA IIPIGGGTSV TNALDTPVTE
KRMVISLDMA LLDKILWIDR ENLTCRAQAG IVGQSLERQL NKKGFTCGHE PDSIEFSTLG
GWVSTRASGM KKNKYGNIED LIVHLNFVCP KGIIQKQCQV PRMSCGPDIH QVILGSEGTF
GVVSEVTMKI FPLPEVKRYG SFVFPNFESG VNFFRDVARL RIQPASLRLM DNDQFVMGQA
LKVASDSWWA SLKSSVSKMY ITSWKGFKVD EICAATCVYE GSREEVDQQE ERLNKLAAEF
HGVVGGEENG QYGYRLTFAI AYLRDLGMNH GVLGESFETS VPWDKVLSLC RNVKELMRRE
AKAQGVKHPV LASCRVTQVY DAGACVYFYF GFNARGLADG MHVYDRIETA ARDEIIACGG
SISHHHGVGK IRKQWMLTTN GAVGIALLKA IKSELDPANI FANANLIDII GSPHCKL
//
