P41367 (ACADM_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Short name=MCAD
EC=1.3.8.7

Gene names

Name:

ACADM

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell differentiation Inferred from electronic annotation. Source: Compara carnitine biosynthetic process Inferred from electronic annotation. Source: Compara carnitine metabolic process, CoA-linked Inferred from electronic annotation. Source: Compara 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: Compara glycogen biosynthetic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara medium-chain fatty acid metabolic process Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of gluconeogenesis Inferred from electronic annotation. Source: Compara response to cold Inferred from electronic annotation. Source: Compara response to starvation Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from electronic annotation. Source: Compara mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acyl-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: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 25

25

Mitochondrion

Chain

26 – 421

396

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000505

Regions

Nucleotide binding

158 – 167

10

FAD

Nucleotide binding

191 – 193

3

FAD

Nucleotide binding

306 – 308

3

FAD; shared with dimeric partner

Nucleotide binding

316 – 317

2

FAD

Nucleotide binding

374 – 378

5

FAD; shared with dimeric partner

Nucleotide binding

403 – 405

3

FAD

Region

278 – 281

4

Substrate binding

Sites

Active site

401

1

Proton acceptor

Binding site

167

1

Substrate; via carbonyl oxygen

Binding site

216

1

Substrate

Binding site

278

1

Substrate

Binding site

402

1

Substrate; via amide nitrogen

Binding site

413

1

Substrate

Amino acid modifications

Modified residue

279

1

N6-acetyllysine By similarity

Modified residue

301

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

8

1

S → G in AAA83759. Ref.1

Sequence conflict

40

1

E → K in AAA83759. Ref.1

Sequence conflict

283

1

P → S in AAA83759. Ref.1

Sequence conflict

305

1

E → G in AAA83759. Ref.1

Sequence conflict

331

1

E → D in AAA83759. Ref.1

Secondary structure

1

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421

Helix Strand Turn

Details...

Helix

43 – 58

16

Helix

61 – 70

10

Helix

75 – 83

9

Helix

93 – 95

3

Helix

102 – 115

14

Helix

117 – 136

20

Helix

139 – 151

13

Beta strand

156 – 159

4

Beta strand

165 – 167

3

Helix

169 – 171

3

Beta strand

175 – 178

4

Beta strand

180 – 193

14

Turn

194 – 197

4

Beta strand

199 – 206

8

Helix

215 – 218

4

Beta strand

219 – 225

7

Beta strand

231 – 236

6

Beta strand

239 – 242

4

Beta strand

247 – 258

12

Helix

259 – 261

3

Beta strand

262 – 265

4

Helix

269 – 303

35

Helix

313 – 315

3

Helix

317 – 345

29

Helix

351 – 376

26

Helix

378 – 381

4

Helix

387 – 394

8

Helix

395 – 398

4

Beta strand

400 – 402

3

Helix

404 – 417

14

Sequences

	Sequence		Length	Mass (Da)
	P41367 [UniParc]. Last modified May 29, 2007. Version 3. Checksum: 73BC66092D5E02CB	FASTA	421	46,485
	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

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.

RefSeq

NP_999204.1. NM_214039.1.

UniGene

Ssc.142.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P41367.

SMR

P41367. Positions 36-420.

ModBase

Search...

Protein-protein interaction databases

STRING

9823.ENSSSCP00000004085.

Proteomic databases

PaxDb

P41367.

PRIDE

P41367.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSSSCT00000004179; ENSSSCP00000004085; ENSSSCG00000003776.

GeneID

397104.

KEGG

ssc:397104.

Organism-specific databases

CTD

34.

Phylogenomic databases

eggNOG

COG1960.

GeneTree

ENSGT00680000099623.

HOGENOM

HOG000131659.

HOVERGEN

HBG000224.

KO

K00249.

OMA

IAMGTFD.

OrthoDB

EOG4G7BZB.

Enzyme and pathway databases

SABIO-RK

P41367.

UniPathway

UPA00660.

Family and domain databases

Gene3D

1.10.540.10. 1 hit.
2.40.110.10. 1 hit.

InterPro

IPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
[Graphical view]

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]

SUPFAM

SSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.

PROSITE

PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P41367.

Entry information

Entry name

ACADM_PIG

Accession

Primary (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 3, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program