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Reviewed, UniProtKB/Swiss-Prot Q9VSA3 (ACADM_DROME)

Last modified November 4, 2008. Version 67. 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3
Gene names
ORF Names: CG12262
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 length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16 By similarity.

Catalytic activity

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrixBy similarity.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

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Ontologies

Keywords

   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processfatty acid beta-oxidation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentlipid particle

Inferred from direct assay. Source: FlyBase

   Molecular functionacyl-CoA dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

mbtQ9VXE51EBI-87748,EBI-75994

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1717Mitochondrion By similarity
Chain18 – 419402Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000508

Regions

Nucleotide binding154 – 16310FAD By similarity
Nucleotide binding187 – 1893FAD By similarity
Nucleotide binding302 – 3043FAD By similarity
Nucleotide binding312 – 3132FAD By similarity
Nucleotide binding370 – 3745FAD By similarity
Nucleotide binding399 – 4013FAD By similarity
Region274 – 2774Substrate binding By similarity

Sites

Active site3971Proton acceptor By similarity
Binding site1631Substrate; via carbonyl oxygen By similarity
Binding site3981Substrate; via amide nitrogen By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9VSA3-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 0B1970302243C394

FASTA41945,871
        10         20         30         40         50         60 
MAFLNKLAAP ALRQLVSQSR AYAAVSHVSP NGTSFALTED QLQLQELARK FTREEIIPVA 

        70         80         90        100        110        120 
AQYDKSGEYP WPIIKKAWEL GLMNNHIPAD IGGLDLDVFT TCLSAEELAY GCTGIMTALE 

       130        140        150        160        170        180 
ASGLGQTPVI LSGNKEQKKK YLGRLLEEPL VAAYCVTEPG AGSDVSGIKT RAEKKGDEWV 

       190        200        210        220        230        240 
INGQKMWITN GGVANWYFVL ARTNPDPKCP PSKAFTGFIV ERDSPGLTPG RKELNMGQRA 

       250        260        270        280        290        300 
SDTRGITFED VRVPKENVLI GEGAGFKIAM GTFDKTRPPV AAGAVGLAQR CLDEALKYAL 

       310        320        330        340        350        360 
ERKTFGVPIA YHQAVQFMLA DMAIGVETSR LAWRLSAWEI DQGRRNSYYA SIAKCHAADM 

       370        380        390        400        410 
ANKIASDAVQ IFGGNGFNSE YPVEKLMRDA KIYQIYEGTS QIQRLIISRN MYEAAKGQA

« 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: Embryo.

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Cross-references

Sequence databases

AE014296 Genomic DNA. Translation: AAF50524.1.
AY089546 mRNA. Translation: AAL90284.1.
RefSeqNP_648149.1.
UniGeneDm.879

3D structure databases

HSSPHSSP built from PDB template 3MDE based on UniProtKB P41367.
SMRQ9VSA3. Positions 32-409.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:20518N.
IntActQ9VSA3.

Genome annotation databases

EnsemblCG12262. Drosophila melanogaster. [Contig view]
GeneID38864.
KEGGdme:Dmel_CG12262.
NMPDRfig|7227.3.peg.8730.

Organism-specific databases

FlyBaseFBgn0035811. CG12262.

Phylogenomic databases

HOGENOMQ9VSA3.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-015630-MON.

Gene expression databases

ArrayExpressQ9VSA3.
GermOnlineCG12262. Drosophila melanogaster.

Family and domain databases

InterProIPR006091. Acyl-CoA_DHase/Oxase_M.
IPR006089. Acyl-CoA_DHase_CS.
IPR006092. Acyl-CoA_DHase_N.
IPR006090. Acyl-CoA_Oxase/DHase_1.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio810749.

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Entry information

Entry nameACADM_DROME
AccessionPrimary (citable) accession number: Q9VSA3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 2000
Last modified: November 4, 2008
This is version 67 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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents