Skip Header

Contribute Send feedback
Read comments (?) or add your own

O96759 (ADAS_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkyldihydroxyacetonephosphate synthase
Short name=Alkyl-DHAP synthase
EC=2.5.1.26
Alternative name(s):
Alkylglycerone-phosphate synthase
Gene names
Name:eapA
ORF Names:DDB_G0286183
OrganismDictyostelium discoideum (Slime mold)
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.

Cofactor

FAD. Ref.3

Pathway

Glycerolipid metabolism; ether lipid biosynthesis.

Subcellular location

Peroxisome.

Sequence similarities

Belongs to the FAD-binding oxidoreductase/transferase type 4 family.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 611611Alkyldihydroxyacetonephosphate synthase
PRO_0000128178

Regions

Domain137 – 317181FAD-binding PCMH-type
Motif609 – 6113Microbody targeting signal Potential

Sites

Active site5081 Ref.3

Experimental info

Mutagenesis3521R → H: 30-fold reduction in activity. Ref.3
Mutagenesis4471R → L: Loss of activity. The FAD binds poorly to the mutant enzyme. Ref.3
Mutagenesis5081Y → F: Loss of activity. Ref.3
Mutagenesis5441H → I: Loss of activity. Ref.3
Mutagenesis5451H → I: Loss of activity. Ref.3
Mutagenesis5461H → I: Loss of activity. Ref.3

Secondary structure

1 ......................................................................................... 611
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O96759 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 99B1221683350271

FASTA61169,408
        10         20         30         40         50         60 
MSGEKKEYPK EHIDLYQQIK WNGWGDTRKF LHQLKPSGTI AMTTPEVSSV PLPSLRGFIK 

        70         80         90        100        110        120 
KELTLPGEED KPFVLDETPA LQIENIHVDP PKQYPEFVRE LKAFFLPDQL KDDKLARITH 

       130        140        150        160        170        180 
TFGKSLRDLI RVRIGQVKNA PDLIVLPHSH EEVERLVQLA HKYNVVIIPM GGGSNIVGAI 

       190        200        210        220        230        240 
EPVSNERFTV SIDMRRMNKV LWVDRREMTA CIQVGIMGPE LEKQLHKQGV SLGHDPDSFE 

       250        260        270        280        290        300 
FSTLGGWLAT CSSGHQSDKY GDIEDMAVSF RTVTPTGTLE LRNGARSGAG INYKHIILGS 

       310        320        330        340        350        360 
EGTLGIITEA VMKVHAVPQA VEYYGFLFPT FAHAVSALQQ IRSSEVIPTM IRVYDPEETQ 

       370        380        390        400        410        420 
LSFAWKPSKG AVSEFTSAMV KKYLHYIRSF DFKNVCLSII GFEGPKKVVD FHRTSVFDIL 

       430        440        450        460        470        480 
SKNAAFGLGS APGKTWAEKR YDLPYIRDFL LDHNMWVDVA ETTVSYANLQ TLWKDAKQTF 

       490        500        510        520        530        540 
VKHFKDQGIP AWICAHISHT YTNGVCLYFI FASKQNENKD MAQYIEAKKL MTDIIFKYGG 

       550        560        570        580        590        600 
SLSHHHGVGY EHVPWMTRYA TRGWINVYRS LKETIDPKDI CNPRKLIPTI KEENNKEPFL 

       610 
FDVVNVKYPK L

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of alkyl-dihydroxyacetonephosphate synthase cDNA from Dictyostelium discoideum."
de Vet E.C.J.M., van den Bosch H.
Biochem. Biophys. Res. Commun. 252:629-633(1998) [PubMed: 9837757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KASSX-3.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed: 15875012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder."
Razeto A., Mattiroli F., Carpanelli E., Aliverti A., Pandini V., Coda A., Mattevi A.
Structure 15:683-692(2007) [PubMed: 17562315] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 9-587, COFACTOR, ACTIVE SITE, MUTAGENESIS OF ARG-352; ARG-447; TYR-508; HIS-544; HIS-545 AND HIS-546.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ010740 mRNA. Translation: CAA09333.1.
AAFI02000085 Genomic DNA. Translation: EAL64267.1.
PIRJE0365.
RefSeqXP_637836.1. XM_632744.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UUUX-ray1.95A/B/C/D9-587[»]
2UUVX-ray1.99A/B/C/D9-587[»]
ProteinModelPortalO96759.
SMRO96759. Positions 9-586.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29370N.
STRINGO96759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191146; DDB0191146; DDB_G0286183.
GeneID8625550.
GenomeReviewsGene locus eapA in contig CM000153_GR.
KEGGddi:DDB_G0286183.

Organism-specific databases

dictyBaseDDB_G0286183. agps.

Phylogenomic databases

eggNOGKOG1233.
GeneTreeEPrGT00050000005587.
HOGENOMHBG321725.
OMAHSGACLY.
PhylomeDBO96759.
ProtClustDBCLSZ2430123.

Family and domain databases

InterProIPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR016168. FAD-linked_Oxase_FAD-bd_sub2.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
Gene3DG3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
G3DSA:1.10.45.10. Vanillyl_alc_oxidase_C-sub2. 1 hit.
KOK00803.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADAS_DICDI
AccessionPrimary (citable) accession number: O96759
Secondary accession number(s): Q54LZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: November 16, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents