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P41367

- ACADM_PIG

UniProt

P41367 - ACADM_PIG

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Protein
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene
ACADM
Organism
Sus scrofa (Pig)
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
Binding sitei216 – 2161Substrate
Binding sitei278 – 2781Substrate
Active sitei401 – 4011Proton acceptor
Binding sitei402 – 4021Substrate; via amide nitrogen
Binding sitei413 – 4131Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD
Nucleotide bindingi191 – 1933FAD
Nucleotide bindingi306 – 3083FAD; shared with dimeric partner
Nucleotide bindingi316 – 3172FAD
Nucleotide bindingi374 – 3785FAD; shared with dimeric partner
Nucleotide bindingi403 – 4053FAD

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: InterPro
  3. medium-chain-acyl-CoA dehydrogenase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. cardiac muscle cell differentiation Source: Ensembl
  2. carnitine biosynthetic process Source: Ensembl
  3. carnitine metabolic process, CoA-linked Source: Ensembl
  4. fatty acid beta-oxidation Source: UniProtKB
  5. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
  6. glycogen biosynthetic process Source: Ensembl
  7. liver development Source: Ensembl
  8. medium-chain fatty acid catabolic process Source: Ensembl
  9. post-embryonic development Source: Ensembl
  10. regulation of gluconeogenesis Source: Ensembl
  11. response to cold Source: Ensembl
  12. response to starvation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_226431. PPARA activates gene expression.
SABIO-RKP41367.
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 6

Subcellular locationi

GO - Cellular componenti

  1. axon Source: Ensembl
  2. mitochondrial matrix Source: UniProtKB-SubCell
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_0000000505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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 residuei279 – 2791N6-acetyllysine 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

PaxDbiP41367.
PRIDEiP41367.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000004085.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5816
Helixi61 – 7010
Helixi75 – 839
Helixi93 – 953
Helixi102 – 11514
Helixi117 – 13620
Helixi139 – 15113
Beta strandi156 – 1594
Beta strandi165 – 1673
Helixi169 – 1713
Beta strandi175 – 1784
Beta strandi180 – 19314
Turni194 – 1974
Beta strandi199 – 2068
Helixi215 – 2184
Beta strandi219 – 2257
Beta strandi231 – 2366
Beta strandi239 – 2424
Beta strandi247 – 25812
Helixi259 – 2613
Beta strandi262 – 2654
Helixi269 – 30335
Helixi313 – 3153
Helixi317 – 34529
Helixi351 – 37626
Helixi378 – 3814
Helixi387 – 3948
Helixi395 – 3984
Beta strandi400 – 4023
Helixi404 – 41714

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UDYX-ray2.40A/B/C/D26-421[»]
3MDDX-ray2.40A/B36-420[»]
3MDEX-ray2.40A/B36-420[»]
ProteinModelPortaliP41367.
SMRiP41367. Positions 36-420.

Miscellaneous databases

EvolutionaryTraceiP41367.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00750000117417.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG74FF0S.
TreeFamiTF105020.

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.

P41367-1 [UniParc]FASTAAdd to Basket

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MAAMFRRSCR VLRSLSHFGW RSQHTKAVPQ CEPGSGFSFE LTEQQKEFQA    50
TARKFAREEI IPVAAEYDRT GEYPVPLLKR AWELGLMNTH IPESFGGLGL 100
GIIDSCLITE ELAYGCTGVQ TAIEANTLGQ VPLIIGGNYQ QQKKYLGRMT 150
EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW 200
YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKEINM GQRCSDTRGI 250
VFEDVRVPKE NVLTGEGAGF KIAMGTFDKT RPPVAAGAVG LAQRALDEAT 300
KYALERKTFG KLLAEHQGIS FLLADMAMKV ELARLSYQRA AWEIDSGRRN 350
TYYASIAKAY AADIANQLAT DAVQVFGGNG FNTEYPVEKL MRDAKIYQIY 400
EGTAQIQRII IAREHIGRYK N 421
Length:421
Mass (Da):46,485
Last modified:May 29, 2007 - v3
Checksum:i73BC66092D5E02CB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81S → G in AAA83759. 1 Publication
Sequence conflicti40 – 401E → K in AAA83759. 1 Publication
Sequence conflicti283 – 2831P → S in AAA83759. 1 Publication
Sequence conflicti305 – 3051E → G in AAA83759. 1 Publication
Sequence conflicti331 – 3311E → D in AAA83759. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40845 mRNA. Translation: AAA83759.1.
AY705916 mRNA. Translation: AAW30430.1.
RefSeqiNP_999204.1. NM_214039.1.
UniGeneiSsc.142.

Genome annotation databases

EnsembliENSSSCT00000004179; ENSSSCP00000004085; ENSSSCG00000003776.
GeneIDi397104.
KEGGissc:397104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U40845 mRNA. Translation: AAA83759.1 .
AY705916 mRNA. Translation: AAW30430.1 .
RefSeqi NP_999204.1. NM_214039.1.
UniGenei Ssc.142.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UDY X-ray 2.40 A/B/C/D 26-421 [» ]
3MDD X-ray 2.40 A/B 36-420 [» ]
3MDE X-ray 2.40 A/B 36-420 [» ]
ProteinModelPortali P41367.
SMRi P41367. Positions 36-420.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9823.ENSSSCP00000004085.

Proteomic databases

PaxDbi P41367.
PRIDEi P41367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000004179 ; ENSSSCP00000004085 ; ENSSSCG00000003776 .
GeneIDi 397104.
KEGGi ssc:397104.

Organism-specific databases

CTDi 34.

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00750000117417.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
KOi K00249.
OMAi SAWEVDQ.
OrthoDBi EOG74FF0S.
TreeFami TF105020.

Enzyme and pathway databases

UniPathwayi UPA00660 .
Reactomei REACT_226431. PPARA activates gene expression.
SABIO-RK P41367.

Miscellaneous databases

EvolutionaryTracei P41367.

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. 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.

Entry informationi

Entry nameiACADM_PIG
AccessioniPrimary (citable) accession number: P41367
Secondary accession number(s): Q58XQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 29, 2007
Last modified: September 3, 2014
This is version 113 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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