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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

Organism
Sus scrofa (Pig)
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

Pathway:imitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_273926. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_278620. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_308866. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
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 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

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_0000000505Add
BLAST

Amino acid modifications

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

PaxDbiP41367.
PRIDEiP41367.

Expressioni

Gene expression databases

GenevisibleiP41367. SS.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP41367. 2 interactions.
STRINGi9823.ENSSSCP00000004085.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5816Combined sources
Helixi61 – 7010Combined sources
Helixi75 – 839Combined sources
Helixi93 – 953Combined sources
Helixi102 – 11514Combined sources
Helixi117 – 13620Combined sources
Helixi139 – 15113Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 1713Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi180 – 19314Combined sources
Turni194 – 1974Combined sources
Beta strandi199 – 2068Combined sources
Helixi215 – 2184Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi247 – 25812Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2654Combined sources
Helixi269 – 30335Combined sources
Helixi313 – 3153Combined sources
Helixi317 – 34529Combined sources
Helixi351 – 37626Combined sources
Helixi378 – 3814Combined sources
Helixi387 – 3948Combined sources
Helixi395 – 3984Combined sources
Beta strandi400 – 4023Combined sources
Helixi404 – 41714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41367.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP41367.
KOiK00249.
OMAiIAMGTFD.
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

« Hide

        10         20         30         40         50
MAAMFRRSCR VLRSLSHFGW RSQHTKAVPQ CEPGSGFSFE LTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAAEYDRT GEYPVPLLKR AWELGLMNTH IPESFGGLGL
110 120 130 140 150
GIIDSCLITE ELAYGCTGVQ TAIEANTLGQ VPLIIGGNYQ QQKKYLGRMT
160 170 180 190 200
EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKEINM GQRCSDTRGI
260 270 280 290 300
VFEDVRVPKE NVLTGEGAGF KIAMGTFDKT RPPVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALERKTFG KLLAEHQGIS FLLADMAMKV ELARLSYQRA AWEIDSGRRN
360 370 380 390 400
TYYASIAKAY AADIANQLAT DAVQVFGGNG FNTEYPVEKL MRDAKIYQIY
410 420
EGTAQIQRII IAREHIGRYK N
Length:421
Mass (Da):46,485
Last modified:May 29, 2007 - v3
Checksum:i73BC66092D5E02CB
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
U40845 mRNA. Translation: AAA83759.1.
AY705916 mRNA. Translation: AAW30430.1.
RefSeqiNP_999204.1. NM_214039.1.
UniGeneiSsc.142.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41367. 2 interactions.
STRINGi9823.ENSSSCP00000004085.

Proteomic databases

PaxDbiP41367.
PRIDEiP41367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi34.

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP41367.
KOiK00249.
OMAiIAMGTFD.
OrthoDBiEOG74FF0S.
TreeFamiTF105020.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiREACT_273926. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_278620. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
REACT_308866. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP41367.

Miscellaneous databases

EvolutionaryTraceiP41367.

Gene expression databases

GenevisibleiP41367. SS.

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. 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: July 22, 2015
This is version 123 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

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.