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P41367 (ACADM_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

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

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

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 term3D-structure
Complete 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

Inferred from sequence or structural similarity. Source: UniProtKB

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_functionacyl-CoA dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

flavin 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
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000505

Regions

Nucleotide binding158 – 16710FAD
Nucleotide binding191 – 1933FAD
Nucleotide binding306 – 3083FAD; shared with dimeric partner
Nucleotide binding316 – 3172FAD
Nucleotide binding374 – 3785FAD; shared with dimeric partner
Nucleotide binding403 – 4053FAD
Region278 – 2814Substrate binding

Sites

Active site4011Proton acceptor
Binding site1671Substrate; via carbonyl oxygen
Binding site2161Substrate
Binding site2781Substrate
Binding site4021Substrate; via amide nitrogen
Binding site4131Substrate

Amino acid modifications

Modified residue791N6-acetyllysine 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 residue2591N6-acetyllysine; alternate By similarity
Modified residue2591N6-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

Experimental info

Sequence conflict81S → G in AAA83759. Ref.1
Sequence conflict401E → K in AAA83759. Ref.1
Sequence conflict2831P → S in AAA83759. Ref.1
Sequence conflict3051E → G in AAA83759. Ref.1
Sequence conflict3311E → D in AAA83759. Ref.1

Secondary structure

........................................................ 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41367 [UniParc].

Last modified May 29, 2007. Version 3.
Checksum: 73BC66092D5E02CB

FASTA42146,485
        10         20         30         40         50         60 
MAAMFRRSCR VLRSLSHFGW RSQHTKAVPQ CEPGSGFSFE LTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAAEYDRT GEYPVPLLKR AWELGLMNTH IPESFGGLGL GIIDSCLITE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANTLGQ VPLIIGGNYQ QQKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKEINM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVRVPKE NVLTGEGAGF KIAMGTFDKT RPPVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLAEHQGIS FLLADMAMKV ELARLSYQRA AWEIDSGRRN TYYASIAKAY 

       370        380        390        400        410        420 
AADIANQLAT DAVQVFGGNG FNTEYPVEKL MRDAKIYQIY EGTAQIQRII IAREHIGRYK 


N 

« Hide

References

[1]Suzuki H., Kimura M., Ito T., Murakami Y., Hamasima N., Yasue H.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mutation detection in the porcine ACADM gene."
Jeon J.-T., Park J.-J., Kim J.-H., Lim H.-T., Seo B.-Y., Cho I.-C.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[3]"Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate."
Kim J.-J.P., Wang M., Paschke R.
Proc. Natl. Acad. Sci. U.S.A. 90:7523-7527(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH FAD AND SUBSTRATE.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40845 mRNA. Translation: AAA83759.1.
AY705916 mRNA. Translation: AAW30430.1.
RefSeqNP_999204.1. NM_214039.1.
UniGeneSsc.142.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UDYX-ray2.40A/B/C/D26-421[»]
3MDDX-ray2.40A/B36-420[»]
3MDEX-ray2.40A/B36-420[»]
ProteinModelPortalP41367.
SMRP41367. Positions 36-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000004085.

Proteomic databases

PaxDbP41367.
PRIDEP41367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000004179; ENSSSCP00000004085; ENSSSCG00000003776.
GeneID397104.
KEGGssc:397104.

Organism-specific databases

CTD34.

Phylogenomic databases

eggNOGCOG1960.
GeneTreeENSGT00750000117417.
HOGENOMHOG000131659.
HOVERGENHBG000224.
KOK00249.
OMAIAMGTFD.
OrthoDBEOG74FF0S.
TreeFamTF105020.

Enzyme and pathway databases

SABIO-RKP41367.
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

EvolutionaryTraceP41367.

Entry information

Entry nameACADM_PIG
AccessionPrimary (citable) accession number: P41367
Secondary accession number(s): Q58XQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 29, 2007
Last modified: April 16, 2014
This is version 111 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways