[1]	NUCLEOTIDE SEQUENCE [MRNA]. Suzuki H., Kimura M., Ito T., Murakami Y., Hamasima N., Yasue H.; Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skeletal muscle; Jeon J.-T., Park J.-J., Kim J.-H., Lim H.-T., Seo B.-Y., Cho I.-C.; "Mutation detection in the porcine ACADM gene."; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH FAD AND SUBSTRATE. TISSUE=Liver; PubMed=8356049 [NCBI, ExPASy, EBI, Israel, Japan] Kim J.-J.P., Wang M., Paschke R.; "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate."; Proc. Natl. Acad. Sci. U.S.A. 90:7523-7527(1993).

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: Homotetramer.
SUBCELLULAR LOCATION: Mitochondrion matrix.
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

U40845; AAA83759.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY705916; AAW30430.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999204.1; -.

UniGene

Ssc.142

3D structure databases

PDB

1UDY; X-ray; 2.40 A; A/B/C/D=26-421.	[ExPASy / RCSB / EBI]
3MDD; X-ray; 2.40 A; A/B=36-420.	[ExPASy / RCSB / EBI]
3MDE; X-ray; 2.40 A; A/B=36-420.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1UDY; -.
3MDD; -.
3MDE; -.

ModBase

P41367.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from sequence or structural similarity from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

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.

ProtoNet

P41367.

Genome annotation databases

GeneID

397104; -.

KEGG

ssc:397104; -.

Phylogenomic databases

HOVERGEN

P41367; -.

Other

LinkHub

P41367; -.

UniRef

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

Keywords

3D-structure; 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.`
`CHAIN`	`26 421`	`396`	`Medium-chain specific acyl-CoA dehydrogenase, mitochondrial.`	`PRO_0000000505`
`NP_BIND`	`158 167`	`10`	`FAD.`
`NP_BIND`	`191 193`	`3`	`FAD.`
`NP_BIND`	`306 308`	`3`	`FAD.`
`NP_BIND`	`316 317`	`2`	`FAD.`
`NP_BIND`	`374 378`	`5`	`FAD.`
`NP_BIND`	`403 405`	`3`	`FAD.`
`REGION`	`278 281`	`4`	`Substrate binding.`
`ACT_SITE`	`401 401`		`Proton acceptor.`
`BINDING`	`167 167`		`Substrate; via carbonyl oxygen.`
`BINDING`	`216 216`		`Substrate.`
`BINDING`	`349 349`		`Substrate.`
`CONFLICT`	`8 8`		`S -> G (in Ref. 1; AAA83759).`
`CONFLICT`	`40 40`		`E -> K (in Ref. 1; AAA83759).`
`CONFLICT`	`283 283`		`P -> S (in Ref. 1; AAA83759).`
`CONFLICT`	`305 305`		`E -> G (in Ref. 1; AAA83759).`
`CONFLICT`	`331 331`		`E -> D (in Ref. 1; AAA83759).`
`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`
`STRAND`	`156 159`	`4`
`HELIX`	`169 171`	`3`
`STRAND`	`175 178`	`4`
`STRAND`	`180 193`	`14`
`TURN`	`194 197`	`4`
`STRAND`	`199 206`	`8`
`HELIX`	`215 218`	`4`
`STRAND`	`219 225`	`7`
`STRAND`	`231 236`	`6`
`STRAND`	`239 242`	`4`
`STRAND`	`247 258`	`12`
`HELIX`	`259 261`	`3`
`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`
`STRAND`	`400 402`	`3`
`HELIX`	`404 417`	`14`

Sequence information

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

Molecular weight: 46485 Da [This is the MW of the unprocessed precursor]

CRC64: 73BC66092D5E02CB [This is a checksum on the sequence]

        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

P41367 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