ID Q59EI3_HUMAN Unreviewed; 444 AA. AC Q59EI3; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 02-DEC-2020, entry version 88. DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014}; DE EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014}; DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD93065.1}; RN [1] {ECO:0000313|EMBL:BAD93065.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:BAD93065.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RT "Homo sapiens protein coding cDNA."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It CC contains multiple copies of three enzymatic components: branched-chain CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and CC lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00002859, CC ECO:0000256|RuleBase:RU365014}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2- CC methylpropanoyl)transferase]-(R)-N(6)-lipoyl-L-lysine + H(+) = CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-(R)- CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysine + CO2; CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489, CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4; CC Evidence={ECO:0000256|ARBA:ARBA00001381, CC ECO:0000256|RuleBase:RU365014}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|ARBA:ARBA00001964, CC ECO:0000256|RuleBase:RU365014}; CC -!- SUBUNIT: Heterotetramer of alpha and beta chains. CC {ECO:0000256|ARBA:ARBA00011516}. CC -!- SIMILARITY: Belongs to the BCKDHA family. CC {ECO:0000256|ARBA:ARBA00008646, ECO:0000256|RuleBase:RU365014}. 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; AB209828; BAD93065.1; -; mRNA. DR RefSeq; NP_001158255.1; NM_001164783.1. DR MaxQB; Q59EI3; -. DR PeptideAtlas; Q59EI3; -. DR PRIDE; Q59EI3; -. DR GeneID; 593; -. DR CTD; 593; -. DR PharmGKB; PA25297; -. DR BioGRID-ORCS; 593; 6 hits in 842 CRISPR screens. DR GenomeRNAi; 593; -. DR Genevisible; Q59EI3; HS. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IEA:InterPro. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:InterPro. DR InterPro; IPR034616; BCKDH_E1-a. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR029061; THDP-binding. DR PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; SSF52518; 1. PE 2: Evidence at transcript level; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU365014}; Potassium {ECO:0000256|ARBA:ARBA00022958}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, KW ECO:0000256|RuleBase:RU365014}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 106..404 FT /note="E1_dh" FT /evidence="ECO:0000259|Pfam:PF00676" FT REGION 33..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..51 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAD93065.1" SQ SEQUENCE 444 AA; 50400 MW; C5A54AFF6AB9BF87 CRC64; MAVAIAAARV WRLNRGLSQA ALLLLRQPGA RGLARSHPPR QQQQFSSLDD KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIARGPGY GIMSIRVDGN DVFAVYNATK EARRRAVAEN QPFLIEAMTY RIGHHSTSDD SSAYRSVDEV NYWDKQDHPI SRLRHYLLSQ GWWDEEQEKA WRKQSRRKVM EAFEQAERKP KPNPNLLFSD VYQEMPAQLR KQQESLARHL QTYGEHYPLD HFDK //