NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-44, AND SUBCELLULAR LOCATION.
STRAIN=cv. Bintje;
TISSUE=Tuber;
PubMed=11231285 [NCBI, ExPASy, EBI, Israel, Japan]
Faivre-Nitschke S.E., Couee I., Vermel M., Grienenberger J.-M., Gualberto J.M.;
"Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria.";
Eur. J. Biochem. 268:1332-1339(2001).

Comments

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

AJ278988; CAC08234.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P26440; 1IVH. [HSSP ENTRY / PDB]

ModBase

Q9FS87.

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.

Other

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

Keywords

Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 17`	`>17`	`Mitochondrion.`
`CHAIN`	`18 401`	`384`	`Isovaleryl-CoA dehydrogenase 2, mitochondrial.`	`PRO_0000000537`
`ACT_SITE`	`262 262`		`Proton acceptor (By similarity).`
`NON_TER`	`1 1`

Sequence information

Length: 401 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 43970 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 789FF67CA3B4995D [This is a checksum on the sequence]

        10         20         30         40         50         60 
SALFRIKNHQ KPQFAAFSTS LLFDDTQKQF KESVAQFAQE NIAPHAEKID RTNYFPQDVN 

        70         80         90        100        110        120 
LWKLMGDFNL LGITVPEEYG GLGLGYLYHC IAMEEISRAS GSVGLSYGAH TNLCINQLVR 

       130        140        150        160        170        180 
NGTHEQKQKY LPKLISGEHV GALAMSEPDA GSDVVSMKCK ADRVEGGYVL NGNKMWCTNG 

       190        200        210        220        230        240 
PTAQTLVVYA KTDVTASSKG ITAFIIEKGM TGFSTAQKLD KLGMRGSDTC ELVFENCFVP 

       250        260        270        280        290        300 
EENVLGQVGK GVYVLMSGLD LERLVLASGP VGIMQACLDV VLPYVKQREQ FGRPIGEFQF 

       310        320        330        340        350        360 
VQGKVADMYT SMQSSRSYLY SVARECDSGT INTKDCAGVI LSAAERATQV ALQAIQCLGG 

       370        380        390        400 
NGYVNEYPTG RFLRDAKLYE IGAGTSEIRR MIIGRELFKE Q

Q9FS87 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