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A5A6I0 (ACADM_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=MCAD
EC=1.3.8.7
Gene names
Name:ACADM
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

carnitine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

carnitine metabolic process, CoA-linked

Inferred from electronic annotation. Source: Ensembl

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from electronic annotation. Source: Ensembl

glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

medium-chain fatty acid catabolic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of gluconeogenesis

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

medium-chain-acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion By similarity
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000295306

Regions

Nucleotide binding158 – 16710FAD By similarity
Nucleotide binding191 – 1933FAD By similarity
Nucleotide binding306 – 3083FAD By similarity
Nucleotide binding316 – 3172FAD By similarity
Nucleotide binding374 – 3785FAD By similarity
Nucleotide binding403 – 4053FAD By similarity
Region278 – 2814Substrate binding By similarity

Sites

Active site4011Proton acceptor By similarity
Binding site1671Substrate; via carbonyl oxygen By similarity
Binding site2161Substrate By similarity
Binding site4021Substrate; via amide nitrogen By similarity
Binding site4131Substrate By similarity

Amino acid modifications

Modified residue691N6-acetyllysine; alternate By similarity
Modified residue691N6-succinyllysine; alternate By similarity
Modified residue1791N6-succinyllysine By similarity
Modified residue2121N6-acetyllysine; alternate By similarity
Modified residue2121N6-succinyllysine; alternate By similarity
Modified residue2171N6-acetyllysine; alternate By similarity
Modified residue2171N6-succinyllysine; alternate By similarity
Modified residue2711N6-acetyllysine; alternate By similarity
Modified residue2711N6-succinyllysine; alternate By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3011N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5A6I0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: AF7FDB95417441DE

FASTA42146,607
        10         20         30         40         50         60 
MAAGFGRCCR VLRSISRFQW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVKVPRE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF 

       370        380        390        400        410        420 
AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK 


N 

« Hide

References

[1]"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cerebellum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB222108 mRNA. Translation: BAF62353.1.
RefSeqNP_001104286.1. NM_001110816.1.
UniGenePtr.3961.

3D structure databases

ProteinModelPortalA5A6I0.
SMRA5A6I0. Positions 34-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000001508.

Proteomic databases

PRIDEA5A6I0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000059079; ENSPTRP00000052172; ENSPTRG00000000871.
GeneID469356.
KEGGptr:469356.

Organism-specific databases

CTD34.

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131659.
HOVERGENHBG000224.
KOK00249.
OMAIAMGTFD.
OrthoDBEOG74FF0S.
TreeFamTF105020.

Enzyme and pathway databases

UniPathwayUPA00660.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. 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]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20846770.

Entry information

Entry nameACADM_PANTR
AccessionPrimary (citable) accession number: A5A6I0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: June 12, 2007
Last modified: March 19, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways