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P08503

- ACADM_RAT

UniProt

P08503 - ACADM_RAT

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Protein
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene
Acadm
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

FAD.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygen By similarity
Active sitei401 – 4011Proton acceptor By similarity
Binding sitei402 – 4021Substrate; via amide nitrogen By similarity
Binding sitei413 – 4131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD By similarity
Nucleotide bindingi191 – 1933FAD By similarity
Nucleotide bindingi306 – 3083FAD By similarity
Nucleotide bindingi316 – 3172FAD By similarity
Nucleotide bindingi374 – 3785FAD By similarity
Nucleotide bindingi403 – 4053FAD By 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: 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 – 2525Mitochondrion
Add
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000506Add
BLAST

Amino acid modifications

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

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.

Family & Domainsi

Region

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

Sequence similaritiesi

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

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MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT    50
IARKFAREEI IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL 100
GTFDACLITE ELAYGCTGVQ TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT 150
EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG DEYVINGQKM WITNGGKANW 200
YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM GQRCSDTRGI 250
TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 300
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN 350
TYFASIAKAF AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY 400
EGTAQIQRLI IAREHIEKYK N 421
Length:421
Mass (Da):46,555
Last modified:August 1, 1988 - v1
Checksum:i2CF076F8C919BDE8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
J02791 mRNA. Translation: AAA40670.1 .
PIRi A28436. DERTCM.
RefSeqi NP_058682.2. NM_016986.2.
UniGenei Rn.6302.

3D structure databases

ProteinModelPortali P08503.
SMRi P08503. Positions 34-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08503. 1 interaction.
STRINGi 10116.ENSRNOP00000013238.

Chemistry

ChEMBLi CHEMBL2176828.

Proteomic databases

PaxDbi P08503.
PRIDEi P08503.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24158.
KEGGi rno:24158.

Organism-specific databases

CTDi 34.
RGDi 2012. Acadm.

Phylogenomic databases

eggNOGi COG1960.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi P08503.
KOi K00249.
PhylomeDBi P08503.

Enzyme and pathway databases

UniPathwayi UPA00660 .
SABIO-RK P08503.

Miscellaneous databases

NextBioi 602449.
PROi P08503.

Gene expression databases

Genevestigatori P08503.

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

  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(1987) [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(1991) [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: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 128 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

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