Reviewed, UniProtKB/Swiss-Prot Q9FS88 (IVD1_SOLTU)

Names and origin

Protein names

Recommended name:
    Isovaleryl-CoA dehydrogenase 1, mitochondrial
      Short name=IVD 1
    EC=1.3.99.10

Gene names

Name:

IVD1

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	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity. UniProtKB Q9FS87
Subcellular location	Mitochondrion By similarity UniProtKB Q9FS87.
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
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 – 28	28	Mitochondrion By similarity UniProtKB Q9FS87
	Chain	29 – 412	384	Isovaleryl-CoA dehydrogenase 1, mitochondrial UniProtKB Q9FS87		PRO_0000000536
Regions
	Nucleotide binding	154 – 163	10	FAD By similarity
	Nucleotide binding	187 – 189	3	FAD By similarity
	Nucleotide binding	367 – 371	5	FAD By similarity
	Nucleotide binding	396 – 398	3	FAD By similarity
	Region	209 – 210	2	Substrate binding By similarity
	Region	271 – 274	4	Substrate binding By similarity
	Region	394 – 395	2	Substrate binding By similarity
Sites
	Active site	273	1	Proton acceptor By similarity UniProtKB P26440
	Binding site	163	1	Substrate; via carbonyl oxygen By similarity
	Binding site	264	1	Substrate By similarity
	Binding site	299	1	FAD By similarity
	Binding site	310	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9FS88-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5DA6DF31BECE121A	FASTA	412	45,099
	10 20 30 40 50 60 MHKLFAVRSL SSAIAKNFKS LQNQQAAFST SLLLDDTQKQ FKESVAKFAQ ENIAPYAEKI 70 80 90 100 110 120 DRTNSFPKEI NLWKLMGDFN LHGITAPEEY GGLNLGYLYH CIALEEISRA SGAVAVSYGV 130 140 150 160 170 180 QSNVCINQLV RNGTPDQKQK YLPKLISGDH IGALAMSEPN AGSDVVSMKC RADRVDGGYV 190 200 210 220 230 240 LNGNKMWCTN GPVANTLIVY AKTDTTAGSK GITAFIIEKE MPGFSTAQKL DKLGMRGSDT 250 260 270 280 290 300 CELVFENCFV PKENVLGQEG KGVYVLMSGL DLERLVLAAG PVGIMQACMD IVIPYVRQRE 310 320 330 340 350 360 QFGRPIGEFQ LIQGKLADMY TALQSSRSYV YAVAKDCDNG KIDPKDCSGT ILLAAERATQ 370 380 390 400 410 VALQAIQCLG GNGYINEYPT GRLLRDAKMY EIAAGTSEIR RLVIGRELFK HQ

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]. Strain: cv. Bintje. Tissue: Tuber.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ278987 mRNA. Translation: CAC08233.1.
3D structure databases
SMR	Q9FS88. Positions 34-406.
ModBase	Search...
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

IVD1_SOLTU

Accession

Primary (citable) accession number: Q9FS88

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	March 1, 2001
Last modified:	January 19, 2010
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)