ADAS_DICDI
ID ADAS_DICDI Reviewed; 611 AA.
AC O96759; Q54LZ5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26;
DE AltName: Full=Alkylglycerone-phosphate synthase;
GN Name=eapA; ORFNames=DDB_G0286183;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KASSX-3;
RX PubMed=9837757; DOI=10.1006/bbrc.1998.9670;
RA de Vet E.C.J.M., van den Bosch H.;
RT "Nucleotide sequence of alkyl-dihydroxyacetonephosphate synthase cDNA from
RT Dictyostelium discoideum.";
RL Biochem. Biophys. Res. Commun. 252:629-633(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 9-587 IN COMPLEX WITH FAD AND
RP HEXADECAN-1-OL, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, COFACTOR, ACTIVE
RP SITE, AND MUTAGENESIS OF ARG-352; ARG-447; TYR-508; HIS-544; HIS-545 AND
RP HIS-546.
RX PubMed=17562315; DOI=10.1016/j.str.2007.04.009;
RA Razeto A., Mattiroli F., Carpanelli E., Aliverti A., Pandini V., Coda A.,
RA Mattevi A.;
RT "The crucial step in ether phospholipid biosynthesis: structural basis of a
RT noncanonical reaction associated with a peroxisomal disorder.";
RL Structure 15:683-692(2007).
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:0000269|PubMed:17562315}.
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:17562315};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17562315};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17562315}.
CC -!- INTERACTION:
CC O96759; O96759: eapA; NbExp=2; IntAct=EBI-15641715, EBI-15641715;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; AJ010740; CAA09333.1; -; mRNA.
DR EMBL; AAFI02000085; EAL64267.1; -; Genomic_DNA.
DR PIR; JE0365; JE0365.
DR RefSeq; XP_637836.1; XM_632744.1.
DR PDB; 2UUU; X-ray; 1.95 A; A/B/C/D=9-587.
DR PDB; 2UUV; X-ray; 1.99 A; A/B/C/D=9-587.
DR PDBsum; 2UUU; -.
DR PDBsum; 2UUV; -.
DR AlphaFoldDB; O96759; -.
DR SMR; O96759; -.
DR DIP; DIP-29370N; -.
DR STRING; 44689.DDB0191146; -.
DR PaxDb; O96759; -.
DR EnsemblProtists; EAL64267; EAL64267; DDB_G0286183.
DR GeneID; 8625550; -.
DR KEGG; ddi:DDB_G0286183; -.
DR dictyBase; DDB_G0286183; agps.
DR eggNOG; KOG1233; Eukaryota.
DR HOGENOM; CLU_017779_2_0_1; -.
DR InParanoid; O96759; -.
DR OMA; PRCHDEV; -.
DR PhylomeDB; O96759; -.
DR BRENDA; 2.5.1.26; 1939.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR UniPathway; UPA00781; -.
DR EvolutionaryTrace; O96759; -.
DR PRO; PR:O96759; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005777; C:peroxisome; ISS:dictyBase.
DR GO; GO:0043178; F:alcohol binding; IDA:dictyBase.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IDA:dictyBase.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:dictyBase.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
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 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 3D-structure; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism;
KW Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..611
FT /note="Alkyldihydroxyacetonephosphate synthase"
FT /id="PRO_0000128178"
FT DOMAIN 137..317
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 544..546
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MOTIF 609..611
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 508
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17562315"
FT BINDING 169..175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17562315"
FT BINDING 237..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17562315"
FT BINDING 250..255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17562315"
FT BINDING 301..307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17562315"
FT BINDING 447
FT /ligand="substrate"
FT SITE 352
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250"
FT MUTAGEN 352
FT /note="R->H: 30-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:17562315"
FT MUTAGEN 447
FT /note="R->L: Loss of activity. The FAD binds poorly to the
FT mutant enzyme."
FT /evidence="ECO:0000269|PubMed:17562315"
FT MUTAGEN 508
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17562315"
FT MUTAGEN 544
FT /note="H->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17562315"
FT MUTAGEN 545
FT /note="H->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17562315"
FT MUTAGEN 546
FT /note="H->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17562315"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2UUV"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 319..330
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 331..344
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 376..386
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 406..421
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 443..451
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 466..485
FT /evidence="ECO:0007829|PDB:2UUU"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:2UUU"
FT STRAND 504..514
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 522..537
FT /evidence="ECO:0007829|PDB:2UUU"
FT HELIX 564..575
FT /evidence="ECO:0007829|PDB:2UUU"
SQ SEQUENCE 611 AA; 69408 MW; 99B1221683350271 CRC64;
MSGEKKEYPK EHIDLYQQIK WNGWGDTRKF LHQLKPSGTI AMTTPEVSSV PLPSLRGFIK
KELTLPGEED KPFVLDETPA LQIENIHVDP PKQYPEFVRE LKAFFLPDQL KDDKLARITH
TFGKSLRDLI RVRIGQVKNA PDLIVLPHSH EEVERLVQLA HKYNVVIIPM GGGSNIVGAI
EPVSNERFTV SIDMRRMNKV LWVDRREMTA CIQVGIMGPE LEKQLHKQGV SLGHDPDSFE
FSTLGGWLAT CSSGHQSDKY GDIEDMAVSF RTVTPTGTLE LRNGARSGAG INYKHIILGS
EGTLGIITEA VMKVHAVPQA VEYYGFLFPT FAHAVSALQQ IRSSEVIPTM IRVYDPEETQ
LSFAWKPSKG AVSEFTSAMV KKYLHYIRSF DFKNVCLSII GFEGPKKVVD FHRTSVFDIL
SKNAAFGLGS APGKTWAEKR YDLPYIRDFL LDHNMWVDVA ETTVSYANLQ TLWKDAKQTF
VKHFKDQGIP AWICAHISHT YTNGVCLYFI FASKQNENKD MAQYIEAKKL MTDIIFKYGG
SLSHHHGVGY EHVPWMTRYA TRGWINVYRS LKETIDPKDI CNPRKLIPTI KEENNKEPFL
FDVVNVKYPK L
