Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P08503 (ACADM_RAT)

Last modified June 16, 2009. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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.

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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.

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Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
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 response to copper ion Inferred from expression pattern. Source: RGD response to drug Inferred from expression pattern. Source: RGD response to glucocorticoid stimulus Inferred from expression pattern. Source: RGD response to nutrient Inferred from expression pattern. Source: RGD
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acyl-CoA dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB electron carrier activity Inferred from electronic annotation. Source: InterPro isomerase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 25

Mitochondrion

Chain

26 – 421

396

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000506

Regions

Nucleotide binding

158 – 167

FAD By similarity

Nucleotide binding

191 – 193

FAD By similarity

Nucleotide binding

306 – 308

FAD By similarity

Nucleotide binding

316 – 317

FAD By similarity

Nucleotide binding

374 – 378

FAD By similarity

Nucleotide binding

403 – 405

FAD By similarity

Region

278 – 281

Substrate binding By similarity

Sites

Active site

401

Proton acceptor By similarity

Binding site

167

Substrate; via carbonyl oxygen By similarity

Binding site

402

Substrate; via amide nitrogen By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P08503-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 2CF076F8C919BDE8
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FASTA

421

46,555

        10         20         30         40         50         60 
MAAALRRGYK VLRSVSHFEC RAQHTKPSLK QEPGLGFSFE LTEQQKEFQT IARKFAREEI 

        70         80         90        100        110        120 
IPVAPDYDKS GEYPFPLIKR AWELGLINTH IPESCGGLGL GTFDACLITE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVIIAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYVINGQKM WITNGGKANW YFVLTRSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI TFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYFASIAKAF 

       370        380        390        400        410        420 
AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK 


N

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References

[1]	"Molecular cloning and nucleotide sequence of cDNA encoding the entire precursor of rat liver medium chain acyl coenzyme A dehydrogenase." Matsubara Y., Kraus J.P., Ozasa H., Glassberg R., Finocchiaro G., Ikeda Y., Mole J., Rosenberg L.E., Tanaka K. J. Biol. Chem. 262:10104-10108(1987) [PubMed: 3611054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[2]	"Structurally different rat liver medium-chain acyl CoA dehydrogenases directed by complementary DNAs differing in their 5'-region." Inagaki T., Ohishi N., Tsukagoshi N., Udaka S., Ghisla S., Yagi K. Biochim. Biophys. Acta 1077:285-290(1991) [PubMed: 2029527] [Abstract] Cited for: PROTEIN SEQUENCE OF 11-81.

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Cross-references

Sequence databases
	J02791 mRNA. Translation: AAA40670.1.
IPI	IPI00212015.
PIR	DERTCM. A28436.
RefSeq	NP_058682.1.
UniGene	Rn.6302
3D structure databases
HSSP	HSSP built from PDB template 1EGD based on UniProtKB P11310.
SMR	P08503. Positions 35-421.
ModBase	Search...
Proteomic databases
PRIDE	P08503.
Genome annotation databases
Ensembl	ENSRNOG00000009845. Rattus norvegicus. [Contig view]
GeneID	24158.
KEGG	rno:24158.
Organism-specific databases
RGD	2012. Acadm.
Phylogenomic databases
HOVERGEN	P08503.
Enzyme and pathway databases
BRENDA	1.3.99.3. 248.
Gene expression databases
ArrayExpress	P08503.
GermOnline	ENSRNOG00000009845. Rattus norvegicus.
Family and domain databases
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. 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
NextBio	602449.

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Entry information

Entry name

ACADM_RAT

Accession

Primary (citable) accession number: P08503

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents