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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

Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).By similarity

Catalytic activityi

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

Cofactori

Pathwayi: mitochondrial 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)DescriptionActionsGraphical viewLength
Binding sitei167Substrate; via carbonyl oxygen1
Binding sitei216Substrate1
Binding sitei278Substrate1
Active sitei401Proton acceptor1
Binding sitei402Substrate; via amide nitrogen1
Binding sitei413Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 167FAD10
Nucleotide bindingi191 – 193FAD3
Nucleotide bindingi306 – 308FAD; shared with dimeric partner3
Nucleotide bindingi316 – 317FAD2
Nucleotide bindingi374 – 378FAD; shared with dimeric partner5
Nucleotide bindingi403 – 405FAD3

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

ReactomeiR-SSC-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-SSC-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-SSC-77348. 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
Proteomesi
  • UP000008227 Componenti: Chromosome 6

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 25MitochondrionAdd BLAST25
ChainiPRO_000000050526 – 421Medium-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei179N6-succinyllysineBy similarity1
Modified residuei212N6-acetyllysine; alternateBy similarity1
Modified residuei212N6-succinyllysine; alternateBy similarity1
Modified residuei217N6-acetyllysine; alternateBy similarity1
Modified residuei217N6-succinyllysine; alternateBy similarity1
Modified residuei259N6-acetyllysine; alternateBy similarity1
Modified residuei259N6-succinyllysine; alternateBy similarity1
Modified residuei271N6-acetyllysine; alternateBy similarity1
Modified residuei271N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-acetyllysineBy similarity1
Modified residuei301N6-acetyllysineBy similarity1
Modified residuei351PhosphothreonineBy similarity1

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, Phosphoprotein

Proteomic databases

PaxDbiP41367.
PeptideAtlasiP41367.
PRIDEiP41367.

Expressioni

Gene expression databases

BgeeiENSSSCG00000003776.
GenevisibleiP41367. SS.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP41367. 2 interactors.
STRINGi9823.ENSSSCP00000004085.

Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 58Combined sources16
Helixi61 – 70Combined sources10
Helixi75 – 83Combined sources9
Helixi93 – 95Combined sources3
Helixi102 – 115Combined sources14
Helixi117 – 136Combined sources20
Helixi139 – 151Combined sources13
Beta strandi156 – 159Combined sources4
Beta strandi165 – 167Combined sources3
Helixi169 – 171Combined sources3
Beta strandi175 – 178Combined sources4
Beta strandi180 – 193Combined sources14
Turni194 – 197Combined sources4
Beta strandi199 – 206Combined sources8
Helixi215 – 218Combined sources4
Beta strandi219 – 225Combined sources7
Beta strandi231 – 236Combined sources6
Beta strandi239 – 242Combined sources4
Beta strandi247 – 258Combined sources12
Helixi259 – 261Combined sources3
Beta strandi262 – 265Combined sources4
Helixi269 – 303Combined sources35
Helixi313 – 315Combined sources3
Helixi317 – 345Combined sources29
Helixi351 – 376Combined sources26
Helixi378 – 381Combined sources4
Helixi387 – 394Combined sources8
Helixi395 – 398Combined sources4
Beta strandi400 – 402Combined sources3
Helixi404 – 417Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UDYX-ray2.40A/B/C/D26-421[»]
3MDDX-ray2.40A/B36-420[»]
3MDEX-ray2.40A/B36-420[»]
ProteinModelPortaliP41367.
SMRiP41367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41367.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 281Substrate binding4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP41367.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG091G04BS.
TreeFamiTF105020.

Family and domain databases

Gene3Di1.10.540.10. 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)DescriptionActionsGraphical viewLength
Sequence conflicti8S → G in AAA83759 (Ref. 1) Curated1
Sequence conflicti40E → K in AAA83759 (Ref. 1) Curated1
Sequence conflicti283P → S in AAA83759 (Ref. 1) Curated1
Sequence conflicti305E → G in AAA83759 (Ref. 1) Curated1
Sequence conflicti331E → D in AAA83759 (Ref. 1) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UDYX-ray2.40A/B/C/D26-421[»]
3MDDX-ray2.40A/B36-420[»]
3MDEX-ray2.40A/B36-420[»]
ProteinModelPortaliP41367.
SMRiP41367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP41367. 2 interactors.
STRINGi9823.ENSSSCP00000004085.

Proteomic databases

PaxDbiP41367.
PeptideAtlasiP41367.
PRIDEiP41367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi34.

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP41367.
KOiK00249.
OMAiSAWEVDQ.
OrthoDBiEOG091G04BS.
TreeFamiTF105020.

Enzyme and pathway databases

UniPathwayiUPA00660.
ReactomeiR-SSC-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-SSC-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-SSC-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP41367.

Miscellaneous databases

EvolutionaryTraceiP41367.

Gene expression databases

BgeeiENSSSCG00000003776.
GenevisibleiP41367. SS.

Family and domain databases

Gene3Di1.10.540.10. 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...

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: November 2, 2016
This is version 132 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

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 one 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.