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Reviewed, UniProtKB/Swiss-Prot Q9V778 (ADAS_DROME)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
ORF Names: CG10253
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length631 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

alkylglycerone-phosphate synthase activity

Inferred from electronic annotation. Source: EC

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 631631Alkyldihydroxyacetonephosphate synthase
PRO_0000128179

Regions

Domain155 – 337183FAD-binding PCMH-type
Motif629 – 6313Microbody targeting signal Potential

Sites

Active site5291 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9V778-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AEDD6FDDA6BFB862

FASTA63170,822
        10         20         30         40         50         60 
MAAKRNAVTT EAPESSAPGE GTALALDSRL SKRVESVIPK KRHEALKWFG WGYNDSQFYG 

        70         80         90        100        110        120 
KDGIICFRGE KYPLGGCELP SFTKWVEKKF DLRVDTTKQY PQLPRTYPRP VENAPFLHEL 

       130        140        150        160        170        180 
KGTTQVDYSA EGIDRLVRCH GQTLNDIYSL WHHKFRRIPD LVVWPRCHDE VVQLVRLANK 

       190        200        210        220        230        240 
HNVMLVPFGG GTSVSGAITC PQNESRMICA LDTSQMNRLL WLNRENLTVC FESGIVGQDL 

       250        260        270        280        290        300 
ERVLRSEGLT VGHEPDSYEF STLGGWVATR ASGMKKNVYG NIEDLVVRVR MVTPSGTLER 

       310        320        330        340        350        360 
ECSAPRVSCG PDFNHVILGS EGTLGVITEV VLKVRPLPSL RRYGSLAFPN FEQGVLFMRE 

       370        380        390        400        410        420 
VARRRCQPAS VRLMDNEQFM FGQALKPEKS WWASVVDAMK QRYVTSWKGI DLNQICAATL 

       430        440        450        460        470        480 
LFEGDLKDVQ RQEALIYEIA EKFQGFPAGG QNGERGYILT FVIAYIRDFG LHQGIVAESF 

       490        500        510        520        530        540 
ETSVPWDRCS LLCRSVKQRV VSECSKRSIN YYTISCRVTQ TYDAGACIYF YFGFRSTDVA 

       550        560        570        580        590        600 
DPVELFEAIE HSARDEILSC GGSLSHHHGV GKIRSHWYRN AVTETGSSLY SAAKRHLDPK 

       610        620        630 
NIFALGNLLP LEEAQASPPP PTSSTPPKAK L

« Hide

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References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AE013599 Genomic DNA. Translation: AAF58181.1.
AY094917 mRNA. Translation: AAM11270.1.
RefSeqNP_611006.1.
UniGeneDm.12883

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9V778.

Proteomic databases

PRIDEQ9V778.

Genome annotation databases

EnsemblFBtr0087428; FBpp0086558; FBgn0033983; Drosophila melanogaster. [Genome view]
GeneID36669.
KEGGdme:Dmel_CG10253.
NMPDRfig|7227.3.peg.5321.
UCSCCG10253-RA. d. melanogaster.

Organism-specific databases

FlyBaseFBgn0033983. CG10253.

Phylogenomic databases

HOGENOMQ9V778.
OMAFFFNKKG.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-004696-MON.
BRENDA2.5.1.26. 48.

Gene expression databases

ArrayExpressQ9V778.
GermOnlineCG10253. Drosophila melanogaster.

Family and domain databases

InterProIPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016168. FAD-linked_Oxase_FAD-bd_sub2.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
[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.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio799777.

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Entry information

Entry nameADAS_DROME
AccessionPrimary (citable) accession number: Q9V778
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents