Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VSA3

- ACADM_DROME

UniProt

Q9VSA3 - ACADM_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 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

  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. 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.
ExpressionAtlasiQ9VSA3. differential.

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.
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.
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

        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:
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 ENSGT00760000119007.
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.
ExpressionAtlasi Q9VSA3. differential.

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: October 29, 2014
This is version 113 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