Reviewed, UniProtKB/Swiss-Prot Q9FS87 (IVD2_SOLTU)

Names and origin

Protein names

Recommended name:
    Isovaleryl-CoA dehydrogenase 2, mitochondrial
      Short name=IVD 2
    EC=1.3.99.10

Gene names

Name:

IVD2

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	401 AA.
Sequence status	Fragment.
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. UniProtKB P26440
Pathway	Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
Subunit structure	Homodimer. Ref.1
Subcellular location	Mitochondrion Ref.1.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro isovaleryl-CoA dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 17	›17	Mitochondrion Ref.1
	Chain	18 – 401	384	Isovaleryl-CoA dehydrogenase 2, mitochondrial Ref.1		PRO_0000000537
Regions
	Nucleotide binding	143 – 152	10	FAD By similarity
	Nucleotide binding	176 – 178	3	FAD By similarity
	Nucleotide binding	356 – 360	5	FAD By similarity
	Nucleotide binding	385 – 387	3	FAD By similarity
	Region	198 – 199	2	Substrate binding By similarity
	Region	260 – 263	4	Substrate binding By similarity
	Region	383 – 384	2	Substrate binding By similarity
Sites
	Active site	262	1	Proton acceptor By similarity UniProtKB P26440
	Binding site	152	1	Substrate; via carbonyl oxygen By similarity
	Binding site	253	1	Substrate By similarity
	Binding site	288	1	FAD By similarity
	Binding site	299	1	FAD By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q9FS87-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 789FF67CA3B4995D	FASTA	401	43,970
	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

References

[1]

"Purification, characterization and cloning of isovaleryl-CoA dehydrogenase from higher plant mitochondria." Faivre-Nitschke S.E., Couee I., Vermel M., Grienenberger J.-M., Gualberto J.M. Eur. J. Biochem. 268:1332-1339(2001) [PubMed: 11231285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-44, SUBCELLULAR LOCATION. Strain: cv. Bintje. Tissue: Tuber.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ278988 mRNA. Translation: CAC08234.1.
3D structure databases
SMR	Q9FS87. Positions 23-395.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FS87. 1 interaction.
Enzyme and pathway databases
BRENDA	1.3.99.10. 296.
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_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR013786. AcylCoA_DH/ox_N. IPR009100. AcylCoA_DH/oxidase. 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...

Entry information

Entry name

IVD2_SOLTU

Accession

Primary (citable) accession number: Q9FS87

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	March 1, 2001
Last modified:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)