ID A0A163IZ62_ABSGL Unreviewed; 442 AA.
AC A0A163IZ62;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN Name=ABSGL_01580.1 scaffold 1725 {ECO:0000313|EMBL:SAL96205.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL96205.1};
RN [1] {ECO:0000313|EMBL:SAL96205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL96205.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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|RuleBase:RU365014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
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|RuleBase:RU365014};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|RuleBase:RU365014}.
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DR EMBL; LT550732; SAL96205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163IZ62; -.
DR STRING; 4829.A0A163IZ62; -.
DR InParanoid; A0A163IZ62; -.
DR OMA; EMFEGVY; -.
DR OrthoDB; 952at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 101..396
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 442 AA; 50199 MW; 15A40218EE162166 CRC64;
MLRSSFVRPL HRFASLNKGY SFTAGQKLSY SVLANVQSAE ASKTNVASKW ASEDKFTSDM
TFVQNIEPLK AYRVMDHTGT VLDKSHEPNI TEDFAVNLYK KMSQLHTMDG ILYEAQRQGR
ISFYMTHYGE EATMGTAAAL NAEDMIFGQY RESFMLVYRG FTIDEFVNQC FSNELDYGRG
RQMPIHYGTK KLAFQTISSP LGTQIPQAAG AAYAFKLAGK DACSICFFGE GAASEGDFHA
GLNMAATLNS PTIFFCRNNG FAISTPSSEQ YRGDGIASRG VGYGIDTIRV DGNDVWAVYN
ATKAAREIAV KEKRPILIES MTYRIGHHST SDDSTKYRDR KEVEERAQFD NPITRFRRYL
EQKQWWDQEQ DDAWRKHIKK AVLQSFADAE KKKKPSLDYL FTDVYDEMTP NLIRQKQELD
RLIKEYPEYY PTDDHAPSSS SS
//
