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O97157 (ADAS_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Alkyldihydroxyacetonephosphate synthase

Short name=Alkyl-DHAP synthase
EC=2.5.1.26
Alternative name(s):
Alkylglycerone-phosphate synthase
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Pathway

Glycerolipid metabolism; ether lipid biosynthesis.

Subcellular location

Peroxisome By similarity.

Sequence similarities

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

Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
   Biological processLipid synthesis
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionTransferase
Gene Ontology (GO)
   Biological processlipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionUDP-N-acetylmuramate dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

alkylglycerone-phosphate synthase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 613613Alkyldihydroxyacetonephosphate synthase
PRO_0000128180

Regions

Domain126 – 307182FAD-binding PCMH-type
Motif611 – 6133Microbody targeting signal Potential

Sites

Active site4981 By similarity

Sequences

Sequence LengthMass (Da)Tools
O97157 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 27BA9FBF2EB94E3A

FASTA61369,068
        10         20         30         40         50         60 
MDKRMITDAF EEIKWNGWGD TGVCIKYDEA RQLPIHTNGK PMKHLLKFMK DDVLKVKGEF 

        70         80         90        100        110        120 
KIKPTPGLTK EEAIKRLPPP VVKQPFVDEL RQVLSKDQIR LDAYARLTHI FGKNYRDLWR 

       130        140        150        160        170        180 
VRRGMIDRPP DAVILPNNHD DCVKIMELAQ KHNVVVVPFG GGTNVTGGVE PNPFETRRMV 

       190        200        210        220        230        240 
ISIDMRRMGR MLHIDTESGT AVFEVGVLGP DIDEQLSRYG FMMGHDPDSY AYSTLGGWIA 

       250        260        270        280        290        300 
ARGSGAMSNK YGDIENMILA MRVVTPVGVV ETPLTSRPCG VDLNAMFVGS EGAFGLVTEA 

       310        320        330        340        350        360 
VVKIERLPEV KRYEGWLFPS FEVAFTAFHT CTRKGIHPCT MRLYDEDDTR LSFAASTDSG 

       370        380        390        400        410        420 
LVSTFFSKCF KKYIATVKGW NLSKISLVVV GFEGTKAQTN CQRSELVGVF QAFGATCLGT 

       430        440        450        460        470        480 
KPGNTWQEKK YDLPYLRDFA LAHNFWADVF ETSVLYTDAI HCWRAVKKSF AEVMAENGKN 

       490        500        510        520        530        540 
AWIGCHTAHQ YRFGCCLYFT FIGGQADEND LKIFLQVKKR AMEVMLQHRG NLTHHHGIGY 

       550        560        570        580        590        600 
EHVPWMKRYN GEGGLDAIMK FKKALDPKNI CNPGKLLPSP PSEKETPKAT QARQNREMMF 

       610 
DKMGIPGALQ AHL 

« Hide

References

[1]"Molecular characterization of Trypanosoma brucei alkyl-dihydroxyacetonephosphate synthase."
Zomer A.M.W., Michels P.A.M., Opperdoes F.R.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF119091 Genomic DNA. Translation: AAD19697.1.

3D structure databases

ProteinModelPortalO97157.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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_TRYBB
AccessionPrimary (citable) accession number: O97157
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: October 19, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families