ID MBCD_SOLTU Reviewed; 412 AA. AC Q9FS88; M1CK01; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2013, sequence version 2. DT 02-SEP-2026, entry version 131. DE RecName: Full=2-methylacyl-CoA dehydrogenase, mitochondrial; DE EC=1.3.8.5 {ECO:0000269|PubMed:15574432}; DE AltName: Full=2-methylbutanoyl-CoA dehydrogenase; DE AltName: Full=2-methylbutyryl-CoA dehydrogenase; DE Short=2MBCD; DE AltName: Full=Isovaleryl-CoA dehydrogenase 1; DE Short=St-IVD1; DE Flags: Precursor; GN Name=2MBCD; Synonyms=IVD1; ORFNames=PGSC0003DMG400026901; OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum. OX NCBI_TaxID=4113 {ECO:0000312|EMBL:CAC08233.1}; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=cv. Bintje; TISSUE=Tuber; RX PubMed=11231285; DOI=10.1046/j.1432-1327.2001.01999.x; RA Faivre-Nitschke S.E., Couee I., Vermel M., Grienenberger J.-M., RA Gualberto J.M.; RT "Purification, characterization and cloning of isovaleryl-CoA dehydrogenase RT from higher plant mitochondria."; RL Eur. J. Biochem. 268:1332-1339(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. DM1-3 516 R44; RX PubMed=21743474; DOI=10.1038/nature10158; RG The Potato Genome Sequencing Consortium; RT "Genome sequence and analysis of the tuber crop potato."; RL Nature 475:189-195(2011). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP SUBSTRATE SPECIFICITY, AND 3D-STRUCTURE MODELING. RX PubMed=15574432; DOI=10.1074/jbc.m412640200; RA Goetzman E.S., Mohsen A.W., Prasad K., Vockley J.; RT "Convergent evolution of a 2-methylbutyryl-CoA dehydrogenase from RT isovaleryl-CoA dehydrogenase in Solanum tuberosum."; RL J. Biol. Chem. 280:4873-4879(2005). CC -!- FUNCTION: Short/branched-chain acyl-CoA dehydrogenase (SBCAD). Uses 2- CC methylbutanoyl-CoA as substrate. Minor activity with the straight-chain CC substrates, butanoyl-CoA, valeryl-CoA, hexanoyl-CoA, and octanoyl-CoA CC but no activity with isovaleryl-CoA. {ECO:0000269|PubMed:15574432}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-methylbutanoyl-CoA + oxidized [electron-transfer CC flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced CC [electron-transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA- CC COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57336, ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:58307; EC=1.3.8.5; CC Evidence={ECO:0000269|PubMed:15574432}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P26440}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1 uM for 2-methylbutanoyl-CoA {ECO:0000269|PubMed:15574432}; CC Note=kcat is 1.77 sec(-1) per tetramer for 2-methylbutanoyl-CoA.; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15574432}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11231285}. CC -!- TISSUE SPECIFICITY: Expressed in flowers. CC {ECO:0000269|PubMed:11231285}. CC -!- MISCELLANEOUS: Due to a high homology with IVD, this protein was CC initially thought to be a second copy of the isovaleryl-CoA CC dehydrogenase (PubMed:11231285), but based on 3D-structure modeling and CC mutagenesis of the human isovaleryl-CoA dehydrogenase, Val-116, Val- CC 120, Val-124, Met-389 and Ala-393 were shown to provide the substrate CC specificity for 2-methylbutanoyl-CoA (PubMed:15574432). CC {ECO:0000305|PubMed:11231285, ECO:0000305|PubMed:15574432}. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ278987; CAC08233.1; -; mRNA. DR RefSeq; NP_001275043.1; NM_001288114.1. DR AlphaFoldDB; Q9FS88; -. DR SMR; Q9FS88; -. DR STRING; 4113.Q9FS88; -. DR PaxDb; 4113-Q9FS88; -. DR EnsemblPlants; PGSC0003DMT400069152; PGSC0003DMT400069152; PGSC0003DMG400026901. DR GeneID; 102589539; -. DR Gramene; PGSC0003DMT400069152; PGSC0003DMT400069152; PGSC0003DMG400026901. DR KEGG; sot:102589539; -. DR eggNOG; KOG0141; Eukaryota. DR HOGENOM; CLU_018204_0_1_1; -. DR InParanoid; Q9FS88; -. DR OMA; YNVERMM; -. DR OrthoDB; 9988775at2759; -. DR SABIO-RK; Q9FS88; -. DR Proteomes; UP000011115; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0003853; F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity; IDA:UniProtKB. DR GO; GO:1902192; P:2-methylbut-2-enoyl-CoA(4-) metabolic process; IDA:UniProtKB. DR GO; GO:1902190; P:2-methylbutanoyl-CoA(4-) catabolic process; IDA:UniProtKB. DR CDD; cd01156; IVD; 1. DR FunFam; 1.10.540.10:FF:000007; Isovaleryl-CoA dehydrogenase, mitochondrial; 1. DR FunFam; 2.40.110.10:FF:000004; Isovaleryl-CoA dehydrogenase, mitochondrial; 1. DR FunFam; 1.20.140.10:FF:000003; isovaleryl-CoA dehydrogenase, mitochondrial; 1. DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf. DR InterPro; IPR036250; AcylCo_DH-like_C. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR006091; AcylCoA_DH/ox_M. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf. DR InterPro; IPR034183; IVD. DR PANTHER; PTHR43884:SF27; 2-METHYLACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 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 PIRSF; PIRSF016578; HsaA; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; KW Transit peptide. FT TRANSIT 1..25 FT /note="Mitochondrion" FT /evidence="ECO:0000305" FT CHAIN 26..412 FT /note="2-methylacyl-CoA dehydrogenase, mitochondrial" FT /id="PRO_0000000536" FT ACT_SITE 273 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 154..163 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 187..189 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 209..210 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 264 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 271..274 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 299 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 310 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 367..371 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 394..395 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P26440" FT BINDING 396..398 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P26440" FT CONFLICT 15..17 FT /note="VKS -> AKN (in Ref. 1; CAC08233)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="N -> K (in Ref. 1; CAC08233)" FT /evidence="ECO:0000305" SQ SEQUENCE 412 AA; 45086 MW; B6F7617173C9ABF8 CRC64; MHKLFAVRSL SSAIVKSFKS LQNQQAAFST SLLLDDTQKQ FKESVAKFAQ ENIAPYAEKI DRTNSFPKEI NLWKLMGDFN LHGITAPEEY GGLNLGYLYH CIALEEISRA SGAVAVSYGV QSNVCINQLV RNGTPDQKQK YLPKLISGDH IGALAMSEPN AGSDVVSMKC RADRVDGGYV LNGNKMWCTN GPVANTLIVY AKTDTTAGSK GITAFIIEKE MPGFSTAQKL DKLGMRGSDT CELVFENCFV PNENVLGQEG KGVYVLMSGL DLERLVLAAG PVGIMQACMD IVIPYVRQRE QFGRPIGEFQ LIQGKLADMY TALQSSRSYV YAVAKDCDNG KIDPKDCSGT ILLAAERATQ VALQAIQCLG GNGYINEYPT GRLLRDAKMY EIAAGTSEIR RLVIGRELFK HQ //