ADAS_RAT
ID ADAS_RAT Reviewed; 644 AA.
AC Q9EQR2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26 {ECO:0000269|PubMed:2340111, ECO:0000269|PubMed:8399344};
DE AltName: Full=Alkylglycerone-phosphate synthase;
DE Flags: Precursor;
GN Name=Agps; Synonyms=Ads;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gondcaille C., Bugaut M.;
RT "Cloning of rat alkyl-dihydroxyacetonephosphate synthase.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND ACTIVITY REGULATION.
RX PubMed=2340111; DOI=10.1515/bchm3.1990.371.1.339;
RA Gunawan J., Rabert U., Voelkl A., Debuch H.;
RT "Kinetic studies of alkyl-dihydroxyacetone-phosphate (alkyl-glycerone-
RT phosphate) synthase in peroxisomes of rat liver.";
RL Biol. Chem. Hoppe-Seyler 371:339-344(1990).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8399344; DOI=10.1016/0005-2760(93)90070-p;
RA Zomer A.W., de Weerd W.F., Langeveld J., van den Bosch H.;
RT "Ether lipid synthesis: purification and identification of alkyl
RT dihydroxyacetone phosphate synthase from guinea-pig liver.";
RL Biochim. Biophys. Acta 1170:189-196(1993).
CC -!- FUNCTION: Catalyzes the exchange of the acyl chain in acyl-
CC dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol,
CC yielding the first ether linked intermediate, i.e. alkyl-
CC dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid
CC biosynthesis. {ECO:0000269|PubMed:8399344}.
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:0000269|PubMed:2340111, ECO:0000269|PubMed:8399344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36172;
CC Evidence={ECO:0000305|PubMed:2340111, ECO:0000305|PubMed:8399344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-
CC hexadecylglycerone 3-phosphate + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40659, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16125, ChEBI:CHEBI:58303, ChEBI:CHEBI:77429;
CC Evidence={ECO:0000250|UniProtKB:P97275};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40660;
CC Evidence={ECO:0000250|UniProtKB:P97275};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid
CC = a 1-acylglycerone 3-phosphate + hexadecanoate;
CC Xref=Rhea:RHEA:40727, ChEBI:CHEBI:7896, ChEBI:CHEBI:57534,
CC ChEBI:CHEBI:57560, ChEBI:CHEBI:58303;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40728;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P97275};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cation Mg(2+).
CC {ECO:0000269|PubMed:2340111}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for hexadecanol {ECO:0000269|PubMed:2340111};
CC KM=38 uM for octadecenol {ECO:0000269|PubMed:2340111};
CC KM=50 uM for palmitoylglycerone phosphate
CC {ECO:0000269|PubMed:2340111};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:2340111};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P97275}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P97275}. Peroxisome
CC {ECO:0000269|PubMed:2340111}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; AF121052; AAG43235.1; -; mRNA.
DR RefSeq; NP_445802.2; NM_053350.2.
DR AlphaFoldDB; Q9EQR2; -.
DR SMR; Q9EQR2; -.
DR STRING; 10116.ENSRNOP00000002111; -.
DR iPTMnet; Q9EQR2; -.
DR PhosphoSitePlus; Q9EQR2; -.
DR jPOST; Q9EQR2; -.
DR PaxDb; Q9EQR2; -.
DR PRIDE; Q9EQR2; -.
DR GeneID; 84114; -.
DR KEGG; rno:84114; -.
DR CTD; 8540; -.
DR RGD; 620364; Agps.
DR eggNOG; KOG1233; Eukaryota.
DR InParanoid; Q9EQR2; -.
DR OrthoDB; 824020at2759; -.
DR PhylomeDB; Q9EQR2; -.
DR Reactome; R-RNO-75896; Plasmalogen biosynthesis.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR UniPathway; UPA00781; -.
DR PRO; PR:Q9EQR2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IDA: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; ISO:RGD.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 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; IPR016167; FAD-bd_PCMH_sub1.
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 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Peroxisome; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Peroxisome"
FT /evidence="ECO:0000250"
FT CHAIN 45..644
FT /note="Alkyldihydroxyacetonephosphate synthase,
FT peroxisomal"
FT /id="PRO_0000231677"
FT DOMAIN 188..370
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..603
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT REGION 640..644
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 564
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 220..226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 289..295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 302..305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 354..360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT SITE 405
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0I1"
FT MOD_RES 88
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
SQ SEQUENCE 644 AA; 71587 MW; CF88FFEF0BE20C75 CRC64;
MAEAAGEAGA SERDPDAVRA RRRLRVLSGH LLGRPQEAPS TNECKARRAA SAAGASPAAS
PAAPESGTIP KKRQELMKWN GWGYNDSKFL LNKKGQVELT GKRYPLSGLA LPTLKDWIQN
TLGVNLEHKT TSKPSINPSE APPSIVNEDF LQELKEAHIS YSQDADDRVF RAHGHCLHEI
FLLREGMFER IPDIVVWPTC HDDVVKIVNL ACKYNLCIIP IGGGTSVSYG LMCPADETRT
IISLDTSQMN RILWVDENNL TAHVEAGITG QDLERQLKES GYCTGHEPDS LEFSIVGGWI
STRASGMKKN VYGNIEDLVV HMKMVTPRGV IEKSSQGPRM STGPDIHHFI MGSEGTLGVI
TEATIKIRPT PEYQKYGSVA FPNFEQGVAC LREIAKQRCA PASIRLMDNQ QFQFGHALKP
QVSSIFTSFL DGFKKFYITK FKGFDPNQIS VATLLFEGDR EKVLQHEKQV YDIAAKFGGL
AAGEDNGQRG YLLTYVIAYM RDLGLEYYVV GESFETSAPW DRVIDLCRNV KERIRRECKE
RGVQFAPLST CRVTQTYDAG ACIYFYFAFN YRGISDPLTV FEQTEAAARD EILANGGSLS
HHHGVGKLRK QWLKESISDV GFGMLKSVKD YVDPSNIFGN RNLL
