Reviewed, UniProtKB/Swiss-Prot P41367 (ACADM_PIG)

Names and origin

Protein names

Recommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3

Gene names

Name:

ACADM

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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	Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
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
Technical term	3D-structure
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyl-CoA dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro
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

Nucleotide binding

316 – 317

2

FAD

Nucleotide binding

374 – 378

5

FAD

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

349

1

Substrate

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

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)
	P41367-1 [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: 8356049] [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

EMBLGenBankDDBJ

U40845 mRNA. Translation: AAA83759.1.
AY705916 mRNA. Translation: AAW30430.1.

RefSeq

NP_999204.1.

UniGene

Ssc.142

3D structure databases

PDBMSD

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

397104.

KEGG

ssc:397104.

Phylogenomic databases

HOVERGEN

P41367.

Family and domain databases

InterPro

IPR006091. Acyl-CoA_DHase/Oxase_M.
IPR006089. Acyl-CoA_DHase_CS.
IPR006092. Acyl-CoA_DHase_N.
IPR006090. Acyl-CoA_Oxase/DHase_1.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]

Gene3D

G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.

Pfam

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

PROSITE

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

ProtoNet

Search...

Other Resources

LinkHub

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:	November 25, 2008
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)