Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alkyldihydroxyacetonephosphate synthase

Gene

eapA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

Pathwayi: ether lipid biosynthesis

This protein is involved in the pathway ether lipid biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway ether lipid biosynthesis and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei352Important for enzyme activityBy similarity1
Binding sitei447Substrate1
Active sitei508Proton donor/acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 175FAD1 Publication7
Nucleotide bindingi237 – 243FAD1 Publication7
Nucleotide bindingi250 – 255FAD1 Publication6
Nucleotide bindingi301 – 307FAD1 Publication7

GO - Molecular functioni

  • alcohol binding Source: dictyBase
  • alkylglycerone-phosphate synthase activity Source: dictyBase
  • FAD binding Source: UniProtKB
  • flavin adenine dinucleotide binding Source: dictyBase
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro

GO - Biological processi

  • ether lipid biosynthetic process Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00781.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyldihydroxyacetonephosphate synthase (EC:2.5.1.26)
Short name:
Alkyl-DHAP synthase
Alternative name(s):
Alkylglycerone-phosphate synthase
Gene namesi
Name:eapA
ORF Names:DDB_G0286183
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0286183. agps.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi352R → H: 30-fold reduction in activity. 1 Publication1
Mutagenesisi447R → L: Loss of activity. The FAD binds poorly to the mutant enzyme. 1 Publication1
Mutagenesisi508Y → F: Loss of activity. 1 Publication1
Mutagenesisi544H → I: Loss of activity. 1 Publication1
Mutagenesisi545H → I: Loss of activity. 1 Publication1
Mutagenesisi546H → I: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001281781 – 611Alkyldihydroxyacetonephosphate synthaseAdd BLAST611

Proteomic databases

PaxDbiO96759.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

DIPiDIP-29370N.
STRINGi44689.DDB0191146.

Structurei

Secondary structure

1611
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 18Combined sources4
Beta strandi21 – 26Combined sources6
Beta strandi30 – 33Combined sources4
Turni35 – 37Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi45 – 47Combined sources3
Helixi55 – 62Combined sources8
Helixi83 – 85Combined sources3
Helixi95 – 102Combined sources8
Helixi107 – 109Combined sources3
Helixi114 – 119Combined sources6
Helixi126 – 133Combined sources8
Beta strandi142 – 145Combined sources4
Helixi150 – 163Combined sources14
Beta strandi166 – 172Combined sources7
Beta strandi189 – 193Combined sources5
Helixi194 – 196Combined sources3
Beta strandi200 – 204Combined sources5
Turni205 – 208Combined sources4
Beta strandi209 – 213Combined sources5
Helixi218 – 227Combined sources10
Helixi239 – 241Combined sources3
Helixi244 – 250Combined sources7
Helixi257 – 260Combined sources4
Helixi263 – 266Combined sources4
Beta strandi267 – 274Combined sources8
Beta strandi277 – 279Combined sources3
Helixi294 – 297Combined sources4
Beta strandi306 – 313Combined sources8
Beta strandi319 – 330Combined sources12
Helixi331 – 344Combined sources14
Beta strandi349 – 354Combined sources6
Helixi356 – 364Combined sources9
Helixi376 – 386Combined sources11
Turni387 – 389Combined sources3
Turni392 – 394Combined sources3
Beta strandi396 – 404Combined sources9
Helixi406 – 421Combined sources16
Turni422 – 424Combined sources3
Beta strandi426 – 432Combined sources7
Helixi435 – 438Combined sources4
Helixi439 – 442Combined sources4
Helixi443 – 451Combined sources9
Turni452 – 454Combined sources3
Beta strandi455 – 465Combined sources11
Helixi466 – 485Combined sources20
Turni486 – 488Combined sources3
Beta strandi491 – 501Combined sources11
Beta strandi504 – 514Combined sources11
Helixi522 – 537Combined sources16
Helixi564 – 575Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UUUX-ray1.95A/B/C/D9-587[»]
2UUVX-ray1.99A/B/C/D9-587[»]
ProteinModelPortaliO96759.
SMRiO96759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO96759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini137 – 317FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni544 – 546Important for enzyme activityBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi609 – 611Microbody targeting signalSequence analysis3

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
InParanoidiO96759.
KOiK00803.
OMAiEIMKWNG.
PhylomeDBiO96759.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR025650. Alkyl-DHAP_Synthase.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PANTHERiPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O96759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGEKKEYPK EHIDLYQQIK WNGWGDTRKF LHQLKPSGTI AMTTPEVSSV
60 70 80 90 100
PLPSLRGFIK KELTLPGEED KPFVLDETPA LQIENIHVDP PKQYPEFVRE
110 120 130 140 150
LKAFFLPDQL KDDKLARITH TFGKSLRDLI RVRIGQVKNA PDLIVLPHSH
160 170 180 190 200
EEVERLVQLA HKYNVVIIPM GGGSNIVGAI EPVSNERFTV SIDMRRMNKV
210 220 230 240 250
LWVDRREMTA CIQVGIMGPE LEKQLHKQGV SLGHDPDSFE FSTLGGWLAT
260 270 280 290 300
CSSGHQSDKY GDIEDMAVSF RTVTPTGTLE LRNGARSGAG INYKHIILGS
310 320 330 340 350
EGTLGIITEA VMKVHAVPQA VEYYGFLFPT FAHAVSALQQ IRSSEVIPTM
360 370 380 390 400
IRVYDPEETQ LSFAWKPSKG AVSEFTSAMV KKYLHYIRSF DFKNVCLSII
410 420 430 440 450
GFEGPKKVVD FHRTSVFDIL SKNAAFGLGS APGKTWAEKR YDLPYIRDFL
460 470 480 490 500
LDHNMWVDVA ETTVSYANLQ TLWKDAKQTF VKHFKDQGIP AWICAHISHT
510 520 530 540 550
YTNGVCLYFI FASKQNENKD MAQYIEAKKL MTDIIFKYGG SLSHHHGVGY
560 570 580 590 600
EHVPWMTRYA TRGWINVYRS LKETIDPKDI CNPRKLIPTI KEENNKEPFL
610
FDVVNVKYPK L
Length:611
Mass (Da):69,408
Last modified:May 1, 1999 - v1
Checksum:i99B1221683350271
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010740 mRNA. Translation: CAA09333.1.
AAFI02000085 Genomic DNA. Translation: EAL64267.1.
PIRiJE0365.
RefSeqiXP_637836.1. XM_632744.1.

Genome annotation databases

EnsemblProtistsiEAL64267; EAL64267; DDB_G0286183.
GeneIDi8625550.
KEGGiddi:DDB_G0286183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010740 mRNA. Translation: CAA09333.1.
AAFI02000085 Genomic DNA. Translation: EAL64267.1.
PIRiJE0365.
RefSeqiXP_637836.1. XM_632744.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UUUX-ray1.95A/B/C/D9-587[»]
2UUVX-ray1.99A/B/C/D9-587[»]
ProteinModelPortaliO96759.
SMRiO96759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29370N.
STRINGi44689.DDB0191146.

Proteomic databases

PaxDbiO96759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL64267; EAL64267; DDB_G0286183.
GeneIDi8625550.
KEGGiddi:DDB_G0286183.

Organism-specific databases

dictyBaseiDDB_G0286183. agps.

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
InParanoidiO96759.
KOiK00803.
OMAiEIMKWNG.
PhylomeDBiO96759.

Enzyme and pathway databases

UniPathwayiUPA00781.

Miscellaneous databases

EvolutionaryTraceiO96759.
PROiO96759.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR025650. Alkyl-DHAP_Synthase.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
PANTHERiPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADAS_DICDI
AccessioniPrimary (citable) accession number: O96759
Secondary accession number(s): Q54LZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: November 2, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.