NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cerebellum;
DOI=10.1016/j.gene.2007.04.013; PubMed=17574350 [NCBI, ExPASy, EBI, Israel, Japan]
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome.";
Gene 399:1-10(2007).

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

AB222108; BAF62353.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001104286.1; -.

3D structure databases

ModBase

A5A6I0.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006631;	Biological process: fatty acid metabolic process (inferred from electronic annotation from UniProtKB-KW).
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.
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

ENSPTRG00000000871; Pan troglodytes. [Contig view]

GeneID

469356; -.

KEGG

ptr:469356; -.

Other

ProtoNet

A5A6I0.

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_0000295306`
`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: 46607 Da [This is the MW of the unprocessed precursor]

CRC64: AF7FDB95417441DE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAGFGRCCR VLRSISRFQW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVKVPRE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF 

       370        380        390        400        410        420 
AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK 


N

A5A6I0 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