[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 3-methylbutanoyl-CoA + acceptor = 3-methylbut-2-enoyl-CoA + reduced acceptor.
COFACTOR: FAD (By similarity).
PATHWAY: Amino-acid degradation; L-leucine degradation; HMG-CoA from 3-isovaleryl-CoA: step 1/3 .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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

BC102836; AAI02837.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001029554.1; -.

UniGene

Bt.49071

3D structure databases

SMR

Q3SZI8; 38-424.

ModBase

Q3SZI8.

Protein-protein interaction databases

IntAct

Q3SZI8; -.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
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

Q3SZI8.

Genome annotation databases

Ensembl

ENSBTAG00000004409; Bos taurus. [Contig view]

GeneID

510440; -.

KEGG

bta:510440; -.

Phylogenomic databases

HOVERGEN

Q3SZI8; -.

Other

ProtoNet

Q3SZI8.

UniRef

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

Keywords

Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 32`	`32`	`Mitochondrion (By similarity).`
`CHAIN`	`33 426`	`394`	`Isovaleryl-CoA dehydrogenase, mitochondrial.`	`PRO_0000281993`
`ACT_SITE`	`286 286`		`Proton acceptor (By similarity).`
`MOD_RES`	`78 78`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 46498 Da [This is the MW of the unprocessed precursor]

CRC64: 77C268E25568ACCA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAAWLLGR RVASWRMRPP LQSLAGLITQ RTNSLLPVDD AVNGLNEEQK QLRQTVAKFL 

        70         80         90        100        110        120 
QEHLAPQAQE IDQSNEFKNL REFWKQLGNL GVLGITAPVQ YGGSGLGFLE NVLVMEEISR 

       130        140        150        160        170        180 
VSGAVGLSYG AHSNLCINQI VRNGNETQKE KYLPKLISGE YIGALAMSEP NAGSDVVSMK 

       190        200        210        220        230        240 
LKAEKKGDHY VLNGNKFWIT NGPDADVLVV YAKTDVTAVP ASRGITAFIV EKGMPGFSTS 

       250        260        270        280        290        300 
KKLDKLGMRG SNTCELVFED CEVPAANILG HLGKGVYVLM SGLDLERLVL AGGPLGIMQA 

       310        320        330        340        350        360 
VLDHTIPYLH MREAFGQKIG HFQLMQGKMA DMYTRLMACR QYVYNVAKAC DEGHCTTKDC 

       370        380        390        400        410        420 
AGVILYSAEC ATQVALDGIQ CLGGNGYIND FPMGRFLRDA KLYEIGAGTS EVRRLVIGRA 


FNADFH

Q3SZI8 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