ID IVD2_SOLTU Reviewed; 401 AA. AC Q9FS87; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 04-NOV-2008, entry version 51. DE RecName: Full=Isovaleryl-CoA dehydrogenase 2, mitochondrial; DE Short=IVD 2; DE EC=1.3.99.10; DE Flags: Precursor; Fragment; GN Name=IVD2; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-44, AND SUBCELLULAR RP LOCATION. RC STRAIN=cv. Bintje; TISSUE=Tuber; RX MEDLINE=21153238; PubMed=11231285; RA Faivre-Nitschke S.E., Couee I., Vermel M., Grienenberger J.-M., RA Gualberto J.M.; RT "Purification, characterization and cloning of isovaleryl-CoA RT dehydrogenase from higher plant mitochondria."; RL Eur. J. Biochem. 268:1332-1339(2001). CC -!- CATALYTIC ACTIVITY: 3-methylbutanoyl-CoA + acceptor = 3-methylbut- CC 2-enoyl-CoA + reduced acceptor. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; HMG-CoA CC from 3-isovaleryl-CoA: step 1/3. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ278988; CAC08234.1; -; mRNA. DR HSSP; P26440; 1IVH. DR IntAct; Q9FS87; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR006091; Acyl-CoA_DHase/Oxase_M. DR InterPro; IPR006089; Acyl-CoA_DHase_CS. DR InterPro; IPR006092; Acyl-CoA_DHase_N. DR InterPro; IPR006090; Acyl-CoA_Oxase/DHase_1. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C. DR Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1. DR Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1. DR Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; KW Oxidoreductase; Transit peptide. FT TRANSIT <1 17 Mitochondrion. FT CHAIN 18 401 Isovaleryl-CoA dehydrogenase 2, FT mitochondrial. FT /FTId=PRO_0000000537. FT ACT_SITE 262 262 Proton acceptor (By similarity). FT NON_TER 1 1 SQ SEQUENCE 401 AA; 43970 MW; 789FF67CA3B4995D CRC64; SALFRIKNHQ KPQFAAFSTS LLFDDTQKQF KESVAQFAQE NIAPHAEKID RTNYFPQDVN LWKLMGDFNL LGITVPEEYG GLGLGYLYHC IAMEEISRAS GSVGLSYGAH TNLCINQLVR NGTHEQKQKY LPKLISGEHV GALAMSEPDA GSDVVSMKCK ADRVEGGYVL NGNKMWCTNG PTAQTLVVYA KTDVTASSKG ITAFIIEKGM TGFSTAQKLD KLGMRGSDTC ELVFENCFVP EENVLGQVGK GVYVLMSGLD LERLVLASGP VGIMQACLDV VLPYVKQREQ FGRPIGEFQF VQGKVADMYT SMQSSRSYLY SVARECDSGT INTKDCAGVI LSAAERATQV ALQAIQCLGG NGYVNEYPTG RFLRDAKLYE IGAGTSEIRR MIIGRELFKE Q //