MBCD_SOLTU
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 03-AUG-2022, entry version 118.
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 + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, 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=1.0 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}.
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DR EMBL; AJ278987; CAC08233.1; -; mRNA.
DR RefSeq; NP_001275043.1; NM_001288114.1.
DR AlphaFoldDB; Q9FS88; -.
DR SMR; Q9FS88; -.
DR STRING; 4113.PGSC0003DMT400069152; -.
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; TRQVFFN; -.
DR OrthoDB; 589058at2759; -.
DR SABIO-RK; Q9FS88; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047119; F:2-methyl-branched-chain-enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003853; F:2-methylacyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102035; F:isobutyryl-CoA:FAD oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008470; F:isovaleryl-CoA dehydrogenase activity; IBA:GO_Central.
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 GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR CDD; cd01156; IVD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034183; IVD.
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 SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 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
