[1]	NUCLEOTIDE SEQUENCE [MRNA]. Li H., Xu S., Gao X., Ren H., Li J.; "Association of bovine ACADM SNP with economic traits."; Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Heart ventricle; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This enzyme is specific for acyl chain lengths of 4 to 16 (By similarity).
CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
COFACTOR: FAD (By similarity).
PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation .
SUBUNIT: 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.
SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

EU009460; ABS70460.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102989; AAI02990.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001068703.1; -.

UniGene

Bt.61205

3D structure databases

SMR

Q3SZB4; 36-420.

ModBase

Q3SZB4.

Ontologies

GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

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.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.

Pfam

PF00441; Acyl-CoA_dh_1; 1.
PF02770; Acyl-CoA_dh_M; 1.
PF02771; Acyl-CoA_dh_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00072; ACYL_COA_DH_1; 1.
PS00073; ACYL_COA_DH_2; 1.

Genome annotation databases

Ensembl

ENSBTAG00000024240; Bos taurus. [Contig view]

GeneID

505968; -.

KEGG

bta:505968; -.

Phylogenomic databases

HOVERGEN

Q3SZB4; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 25`	`25`	`Mitochondrion (By similarity).`
`CHAIN`	`26 421`	`396`	`Medium-chain specific acyl-CoA dehydrogenase, mitochondrial.`	`PRO_0000281995`
`NP_BIND`	`158 167`	`10`	`FAD (By similarity).`
`NP_BIND`	`191 193`	`3`	`FAD (By similarity).`
`NP_BIND`	`306 308`	`3`	`FAD (By similarity).`
`NP_BIND`	`316 317`	`2`	`FAD (By similarity).`
`NP_BIND`	`374 378`	`5`	`FAD (By similarity).`
`NP_BIND`	`403 405`	`3`	`FAD (By similarity).`
`REGION`	`278 281`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`401 401`		`Proton acceptor (By similarity).`
`BINDING`	`167 167`		`Substrate; via carbonyl oxygen (By similarity).`
`BINDING`	`402 402`		`Substrate; via amide nitrogen (By similarity).`

Sequence information

Length: 421 AA [This is the length of the unprocessed precursor]

Molecular weight: 46573 Da [This is the MW of the unprocessed precursor]

CRC64: C43979D54E7A3A8D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIALFRRSCG VLRSLSHFDW RSQHTKTALQ REPGSGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPLAAEYDKT GEYPVPLIKR AWELGLMNTH IPESCGGLGL GTFDSCLISE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEANSLGQ MPVIIAGNDQ QQKKYLGRMT EEPLMCAYCV TEPVAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVRVPKE NVLIGEGAGF KIAMGAFDKT RPPVAAAAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLIEHQGIS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAY 

       370        380        390        400        410        420 
AGDIANQLAS DAVQIFGGNG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIGRYK 


K

Q3SZB4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools