Reviewed, UniProtKB/Swiss-Prot P12007 (IVD_RAT)

Names and origin

Protein names

Recommended name:
    Isovaleryl-CoA dehydrogenase, mitochondrial
      Short name=IVD
    EC=1.3.99.10

Gene names

Name:

Ivd

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Homotetramer.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	leucine metabolic process Ref.1 Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW protein homooligomerization Ref.1 Traceable author statement. Source: RGD
Cellular component	mitochondrial matrix Ref.1 Inferred from direct assay. Source: RGD
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro isovaleryl-CoA dehydrogenase activity Ref.1 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion
	Chain	31 – 424	394	Isovaleryl-CoA dehydrogenase, mitochondrial		PRO_0000000534
Sites
	Active site	284	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	76	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12007-1 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: D09FFD0A88EA5791	FASTA	424	46,435
	10 20 30 40 50 60 MATAVRLLGR RVSSWRLRPL PSPLAVPQRA HSMLPVDDDI NGLNEEQKQL RHTISKFVQE 70 80 90 100 110 120 NLAPKAQEID QSNDFKNLRE FWKQLGSLGV LGITAPVQYG GSGLGYLEHV LVMEEISRAS 130 140 150 160 170 180 AAVGLSYGAH SNLCINQIVR NGNEAQKEKY LPKLISGEFI GALAMSEPNA GSDVVSMRLK 190 200 210 220 230 240 AEKKGDHYVL NGNKFWITNG PDADVLVVYA KTDLTAVPAS RGITAFIVEK DMPGFSTSKK 250 260 270 280 290 300 LDKLGMRGSN TCELVFEDCK VPAANILSQE SKGVYVLMSG LDLERLVLAG GPLGIMQAVL 310 320 330 340 350 360 DHTIPYLHVR EAFGQKIGQF QLMQGKMADM YTRLMACRQY VYNVARACDE GHITAKDCAG 370 380 390 400 410 420 VILYTAECAT QVALDGIQCL GGNGYINDFP MGRFLRDAKL YEIGGGTSEV RRLVIGRAFN ADFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family." Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K. J. Biol. Chem. 264:16321-16331(1989) [PubMed: 2777793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[3]	"Isolation of cDNA clones coding for rat isovaleryl-CoA dehydrogenase and assignment of the gene to human chromosome 15." Kraus J.P., Matsubara Y., Barton D., Yang-Feng T.L., Glassberg R., Ito M., Ikeda Y., Mole J., Francke U., Tanaka K. Genomics 1:264-269(1987) [PubMed: 3446585] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-48.
[4]	Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 119-140; 273-285 AND 400-411, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J05031 mRNA. Translation: AAA41454.1. BC088401 mRNA. Translation: AAH88401.1. M19867 mRNA. Translation: AAA41459.1.
IPI	IPI00193716.
PIR	C34252.
RefSeq	NP_036724.1.
UniGene	Rn.147
3D structure databases
HSSP	HSSP built from PDB template 1IVH based on UniProtKB P26440.
SMR	P12007. Positions 36-422.
ModBase	Search...
Proteomic databases
PRIDE	P12007.
Genome annotation databases
Ensembl	ENSRNOG00000009421. Rattus norvegicus. [Contig view]
GeneID	24513.
KEGG	rno:24513.
NMPDR	fig|10116.3.peg.19461.
Organism-specific databases
RGD	2936. Ivd.
Phylogenomic databases
HOVERGEN	P12007.
OMA	P12007. ELFNETR.
Enzyme and pathway databases
BRENDA	1.3.99.10. 248.
Gene expression databases
ArrayExpress	P12007.
GermOnline	ENSRNOG00000009421. Rattus norvegicus.
Family and domain databases
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006092. Acyl-CoA_DH_N. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_M. IPR013786. AcylCoA_DH/ox_N. IPR013764. AcylCoA_oxidase/DH_1/2_C. [Graphical view]
Gene3D	G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit. G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit. G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. PF02771. Acyl-CoA_dh_N. 1 hit. [Graphical view]
PROSITE	PS00072. ACYL_COA_DH_1. 1 hit. PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	603537.

Entry information

Entry name

IVD_RAT

Accession

Primary (citable) accession number: P12007

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)