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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acadm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygenBy similarity
Active sitei401 – 4011Proton acceptorBy similarity
Binding sitei402 – 4021Substrate; via amide nitrogenBy similarity
Binding sitei413 – 4131SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FADBy similarity
Nucleotide bindingi191 – 1933FADBy similarity
Nucleotide bindingi306 – 3083FADBy similarity
Nucleotide bindingi316 – 3172FADBy similarity
Nucleotide bindingi374 – 3785FADBy similarity
Nucleotide bindingi403 – 4053FADBy similarity

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: UniProtKB
  2. fatty-acyl-CoA binding Source: RGD
  3. flavin adenine dinucleotide binding Source: RGD
  4. identical protein binding Source: BHF-UCL
  5. isomerase activity Source: RGD

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB
  2. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  3. medium-chain fatty acid catabolic process Source: RGD
  4. protein homotetramerization Source: RGD
  5. response to copper ion Source: RGD
  6. response to drug Source: RGD
  7. response to glucocorticoid Source: RGD
  8. response to hormone Source: RGD
  9. response to nutrient Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP08503.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:Acadm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2012. Acadm.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: BHF-UCL
  2. mitochondrial membrane Source: BHF-UCL
  3. mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionAdd
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
Modified residuei69 – 691N6-succinyllysine; alternateBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei179 – 1791N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei271 – 2711N6-acetyllysine; alternateBy similarity
Modified residuei271 – 2711N6-succinyllysine; alternateBy similarity
Modified residuei301 – 3011N6-acetyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity. These sites are deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP08503.
PRIDEiP08503.

Expressioni

Gene expression databases

GenevestigatoriP08503.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP08503. 1 interaction.
STRINGi10116.ENSRNOP00000013238.

Structurei

3D structure databases

ProteinModelPortaliP08503.
SMRiP08503. Positions 34-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP08503.
KOiK00249.
PhylomeDBiP08503.

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.

P08503-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT
60 70 80 90 100
IARKFAREEI IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL
110 120 130 140 150
GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT
160 170 180 190 200
EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG DEYVINGQKM WITNGGKANW
210 220 230 240 250
YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI
260 270 280 290 300
TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN
360 370 380 390 400
TYFASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY
410 420
EGTAQIQRLI IAREHIEKYK N
Length:421
Mass (Da):46,555
Last modified:July 31, 1988 - v1
Checksum:i2CF076F8C919BDE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02791 mRNA. Translation: AAA40670.1.
PIRiA28436. DERTCM.
RefSeqiNP_058682.2. NM_016986.2.
UniGeneiRn.6302.

Genome annotation databases

GeneIDi24158.
KEGGirno:24158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02791 mRNA. Translation: AAA40670.1.
PIRiA28436. DERTCM.
RefSeqiNP_058682.2. NM_016986.2.
UniGeneiRn.6302.

3D structure databases

ProteinModelPortaliP08503.
SMRiP08503. Positions 34-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08503. 1 interaction.
STRINGi10116.ENSRNOP00000013238.

Chemistry

ChEMBLiCHEMBL2176828.

Proteomic databases

PaxDbiP08503.
PRIDEiP08503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24158.
KEGGirno:24158.

Organism-specific databases

CTDi34.
RGDi2012. Acadm.

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP08503.
KOiK00249.
PhylomeDBiP08503.

Enzyme and pathway databases

UniPathwayiUPA00660.
SABIO-RKP08503.

Miscellaneous databases

NextBioi602449.
PROiP08503.

Gene expression databases

GenevestigatoriP08503.

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

  1. "Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase."
    Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y., Mole J., Rosenberg L.E., Tanaka K.
    J. Biol. Chem. 262:10104-10108(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Structurally different rat liver medium-chain acyl CoA dehydrogenases directed by complementary DNAs differing in their 5'-region."
    Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K.
    Biochim. Biophys. Acta 1077:285-290(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-81.

Entry informationi

Entry nameiACADM_RAT
AccessioniPrimary (citable) accession number: P08503
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1988
Last sequence update: July 31, 1988
Last modified: March 3, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.