[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Temporal cortex; Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.; "Isolation and characterization of cDNA for macaque neurological disease genes."; Submitted (APR-2002) 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

AB083301; BAC20580.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11310; 1EGD. [HSSP ENTRY / PDB]

SMR

Q8HXY8; 35-421.

ModBase

Q8HXY8.

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.

BLOCKS

Q8HXY8.

Phylogenomic databases

HOVERGEN

Q8HXY8; -.

Other

ProtoNet

Q8HXY8.

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_0000000503`
`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: 46626 Da [This is the MW of the unprocessed precursor]

CRC64: DDA2F825B5AF9CC0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAFGRCCR VLRSISRFHW RSQHTKADRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAAEYDKT GEYPVPLIRR AWELGLMNPH IPQNCGGLGL GTFDACLISE ELAYGCTGVQ 

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

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

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVKVLKE NVLIGDGAGF KIAMGAFDKT RPTVSSGAVG LAQRALDEAT 

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

       370        380        390        400        410        420 
AGDIANQLAT DAVQIFGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI IAREHIGKYK 


S

Q8HXY8 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