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Q9VSA3

- ACADM_DROME

UniProt

Q9VSA3 - ACADM_DROME

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Protein
Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene
CG12262
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

FAD By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631Substrate; via carbonyl oxygen By similarity
Active sitei397 – 3971Proton acceptor By similarity
Binding sitei398 – 3981Substrate; via amide nitrogen By similarity

Regions

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

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_180846. PPARA activates gene expression.
REACT_202493. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_204741. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_206217. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
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: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035811. CG12262.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. lipid particle Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717Mitochondrion By similarity
Add
BLAST
Chaini18 – 419402Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000508Add
BLAST

Proteomic databases

PaxDbiQ9VSA3.
PRIDEiQ9VSA3.

Expressioni

Gene expression databases

BgeeiQ9VSA3.

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. 1 interaction.
MINTiMINT-814595.
STRINGi7227.FBpp0076520.

Structurei

3D structure databases

ProteinModelPortaliQ9VSA3.
SMRiQ9VSA3. Positions 32-409.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00750000117417.
InParanoidiQ9VSA3.
KOiK00249.
OMAiHIPENCD.
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

MAFLNKLAAP ALRQLVSQSR AYAAVSHVSP NGTSFALTED QLQLQELARK    50
FTREEIIPVA AQYDKSGEYP WPIIKKAWEL GLMNNHIPAD IGGLDLDVFT 100
TCLSAEELAY GCTGIMTALE ASGLGQTPVI LSGNKEQKKK YLGRLLEEPL 150
VAAYCVTEPG AGSDVSGIKT RAEKKGDEWV INGQKMWITN GGVANWYFVL 200
ARTNPDPKCP PSKAFTGFIV ERDSPGLTPG RKELNMGQRA SDTRGITFED 250
VRVPKENVLI GEGAGFKIAM GTFDKTRPPV AAGAVGLAQR CLDEALKYAL 300
ERKTFGVPIA YHQAVQFMLA DMAIGVETSR LAWRLSAWEI DQGRRNSYYA 350
SIAKCHAADM ANKIASDAVQ IFGGNGFNSE YPVEKLMRDA KIYQIYEGTS 400
QIQRLIISRN MYEAAKGQA 419
Length:419
Mass (Da):45,871
Last modified:May 1, 2000 - v1
Checksum:i0B1970302243C394
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE014296 Genomic DNA. Translation: AAF50524.1 .
AY089546 mRNA. Translation: AAL90284.1 .
RefSeqi NP_648149.1. NM_139892.3.
UniGenei Dm.879.

3D structure databases

ProteinModelPortali Q9VSA3.
SMRi Q9VSA3. Positions 32-409.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 64295. 83 interactions.
DIPi DIP-20518N.
IntActi Q9VSA3. 1 interaction.
MINTi MINT-814595.
STRINGi 7227.FBpp0076520.

Proteomic databases

PaxDbi Q9VSA3.
PRIDEi Q9VSA3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076808 ; FBpp0076520 ; FBgn0035811 .
GeneIDi 38864.
KEGGi dme:Dmel_CG12262.
UCSCi CG12262-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0035811. CG12262.

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00750000117417.
InParanoidi Q9VSA3.
KOi K00249.
OMAi HIPENCD.
OrthoDBi EOG74FF0S.
PhylomeDBi Q9VSA3.

Enzyme and pathway databases

UniPathwayi UPA00660 .
Reactomei REACT_180846. PPARA activates gene expression.
REACT_202493. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_204741. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_206217. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.

Miscellaneous databases

GenomeRNAii 38864.
NextBioi 810749.
PROi Q9VSA3.

Gene expression databases

Bgeei Q9VSA3.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. 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 ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 111 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

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