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Protein

Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

CG12262

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FADBy similarity

Pathway: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631Substrate; via carbonyl oxygenBy similarity
Active sitei397 – 3971Proton acceptorBy similarity
Binding sitei398 – 3981Substrate; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi154 – 16310FADBy similarity
Nucleotide bindingi187 – 1893FADBy similarity
Nucleotide bindingi302 – 3043FADBy similarity
Nucleotide bindingi312 – 3132FADBy similarity
Nucleotide bindingi370 – 3745FADBy similarity
Nucleotide bindingi399 – 4013FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_279068. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_308693. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_344121. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
ORF Names:CG12262
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035811. CG12262.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionBy similarityAdd
BLAST
Chaini18 – 419402Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000508Add
BLAST

Proteomic databases

PaxDbiQ9VSA3.
PRIDEiQ9VSA3.

Expressioni

Gene expression databases

BgeeiQ9VSA3.
GenevisibleiQ9VSA3. DM.

Interactioni

Subunit structurei

Homotetramer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
mbtQ9VXE51EBI-87748,EBI-75994

Protein-protein interaction databases

BioGridi64295. 83 interactions.
DIPiDIP-20518N.
IntActiQ9VSA3. 6 interactions.
MINTiMINT-814595.
STRINGi7227.FBpp0076520.

Structurei

3D structure databases

ProteinModelPortaliQ9VSA3.
SMRiQ9VSA3. Positions 32-409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 2774Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
InParanoidiQ9VSA3.
KOiK00249.
OMAiIAMGTFD.
OrthoDBiEOG74FF0S.
PhylomeDBiQ9VSA3.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VSA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLNKLAAP ALRQLVSQSR AYAAVSHVSP NGTSFALTED QLQLQELARK
60 70 80 90 100
FTREEIIPVA AQYDKSGEYP WPIIKKAWEL GLMNNHIPAD IGGLDLDVFT
110 120 130 140 150
TCLSAEELAY GCTGIMTALE ASGLGQTPVI LSGNKEQKKK YLGRLLEEPL
160 170 180 190 200
VAAYCVTEPG AGSDVSGIKT RAEKKGDEWV INGQKMWITN GGVANWYFVL
210 220 230 240 250
ARTNPDPKCP PSKAFTGFIV ERDSPGLTPG RKELNMGQRA SDTRGITFED
260 270 280 290 300
VRVPKENVLI GEGAGFKIAM GTFDKTRPPV AAGAVGLAQR CLDEALKYAL
310 320 330 340 350
ERKTFGVPIA YHQAVQFMLA DMAIGVETSR LAWRLSAWEI DQGRRNSYYA
360 370 380 390 400
SIAKCHAADM ANKIASDAVQ IFGGNGFNSE YPVEKLMRDA KIYQIYEGTS
410
QIQRLIISRN MYEAAKGQA
Length:419
Mass (Da):45,871
Last modified:May 1, 2000 - v1
Checksum:i0B1970302243C394
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50524.1.
AY089546 mRNA. Translation: AAL90284.1.
RefSeqiNP_648149.1. NM_139892.3.
UniGeneiDm.879.

Genome annotation databases

EnsemblMetazoaiFBtr0076808; FBpp0076520; FBgn0035811.
GeneIDi38864.
KEGGidme:Dmel_CG12262.
UCSCiCG12262-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50524.1.
AY089546 mRNA. Translation: AAL90284.1.
RefSeqiNP_648149.1. NM_139892.3.
UniGeneiDm.879.

3D structure databases

ProteinModelPortaliQ9VSA3.
SMRiQ9VSA3. Positions 32-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64295. 83 interactions.
DIPiDIP-20518N.
IntActiQ9VSA3. 6 interactions.
MINTiMINT-814595.
STRINGi7227.FBpp0076520.

Proteomic databases

PaxDbiQ9VSA3.
PRIDEiQ9VSA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076808; FBpp0076520; FBgn0035811.
GeneIDi38864.
KEGGidme:Dmel_CG12262.
UCSCiCG12262-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0035811. CG12262.

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
InParanoidiQ9VSA3.
KOiK00249.
OMAiIAMGTFD.
OrthoDBiEOG74FF0S.
PhylomeDBiQ9VSA3.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiREACT_279068. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_308693. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_344121. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.

Miscellaneous databases

GenomeRNAii38864.
NextBioi810749.
PROiQ9VSA3.

Gene expression databases

BgeeiQ9VSA3.
GenevisibleiQ9VSA3. DM.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiACADM_DROME
AccessioniPrimary (citable) accession number: Q9VSA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.