Medium-chain specific acyl-CoA dehydrogenase, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P45952 (ACADM_MOUSE)

Last modified March 2, 2010. Version 96. 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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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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 By similarity.
Pathway	Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
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
PTM	Acetylation
Gene Ontology (GO)
Biological process	cardiac muscle cell differentiation Inferred from mutant phenotype. Source: MGI carnitine metabolic process, CoA-linked Inferred from mutant phenotype. Source: UniProtKB fatty acid beta-oxidation using acyl-CoA dehydrogenase Inferred from mutant phenotype. Source: UniProtKB glycogen biosynthetic process Inferred from mutant phenotype. Source: UniProtKB liver development Inferred from mutant phenotype. Source: MGI medium-chain fatty acid metabolic process Inferred from mutant phenotype. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW post-embryonic development Inferred from mutant phenotype. Source: MGI regulation of gluconeogenesis Inferred from mutant phenotype. Source: UniProtKB response to cold Inferred from mutant phenotype. Source: MGI response to starvation Inferred from mutant phenotype. Source: MGI
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro medium-chain-acyl-CoA dehydrogenase activity Inferred from mutant phenotype. Source: UniProtKB
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 By similarity

Chain

26 – 421

396

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

PRO_0000000504

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

Binding site

413

Substrate By similarity

Amino acid modifications

Modified residue

212

N6-acetyllysine By similarity

Modified residue

301

N6-acetyllysine By similarity

Experimental info

Sequence conflict

135

L → I Ref.2

Sequence conflict

184

V → A Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P45952-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 36976704E3E48CBB
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FASTA

421

46,481

        10         20         30         40         50         60 
MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG 

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

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

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

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


N

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References

[1]	"Molecular cloning and characterization of the mouse medium-chain acyl-CoA dehydrogenase cDNA." Tolwani R.J., Farmer S.C., Wood P.A. Genomics 23:247-249(1994) [PubMed: 7829081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase genes for site-directed mutagenesis of embryonic stem cells." Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P., Johnson L.W., Mountz J.D., Kelly D.P. Prog. Clin. Biol. Res. 375:151-160(1992) [PubMed: 1438358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U07159 mRNA. Translation: AAA76733.1. S48761 Genomic DNA. No translation available. S48759 Genomic DNA. No translation available.
IPI	IPI00134961.
PIR	A55724.
RefSeq	NP_031408.1.
UniGene	Mm.10530
3D structure databases
SMR	P45952. Positions 34-421.
ModBase	Search...
Protein-protein interaction databases
STRING	P45952.
2-D gel databases
SWISS-2DPAGE	P45952.
Proteomic databases
PRIDE	P45952.
Genome annotation databases
Ensembl	ENSMUST00000072697; ENSMUSP00000072483; ENSMUSG00000062908; Mus musculus. [Genome view]
GeneID	11364.
KEGG	mmu:11364.
NMPDR	fig\|10090.3.peg.9178.
UCSC	uc008ruj.1. mouse.
Organism-specific databases
CTD	11364.
MGI	MGI:87867. Acadm.
Phylogenomic databases
eggNOG	roNOG13445.
HOGENOM	HBG699365.
HOVERGEN	HBG000224.
InParanoid	P45952.
OMA	KVELARM.
OrthoDB	EOG9FFGM4.
PhylomeDB	P45952.
Enzyme and pathway databases
BRENDA	1.3.99.3. 244.
Gene expression databases
ArrayExpress	P45952.
Bgee	P45952.
CleanEx	MM_ACADM.
Genevestigator	P45952.
GermOnline	ENSMUSG00000062908. Mus musculus.
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_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. 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]
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 Resources
NextBio	278640.
SOURCE	Search...

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Entry information

Entry name

ACADM_MOUSE

Accession

Primary (citable) accession number: P45952
Secondary accession number(s): Q64235

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	March 2, 2010
This is version 96 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel 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