ID F7RNT0_9GAMM Unreviewed; 351 AA.
AC F7RNT0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=SOHN41_02018 {ECO:0000313|EMBL:EGM69941.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69941.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM69941.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69941.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
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|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|RuleBase:RU365014}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM69941.1}.
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DR EMBL; AFOZ01000024; EGM69941.1; -; Genomic_DNA.
DR AlphaFoldDB; F7RNT0; -.
DR STRING; 327275.SOHN41_02018; -.
DR Proteomes; UP000002956; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 14..309
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 351 AA; 39050 MW; B358041D0146079D CRC64;
MPVIDEALAT KIYDTCVFTR VLDERMLGAQ RQGRISFYMT CTGEEAAIVG SVAALDQEDV
ILAQYREHAA LRYRGFTTEQ FMNQMFSNEK DLGKGRQMPI HYGSAALHYQ TISSPLATQI
PQATGVGYSL KMQGKRNVAV CYFGEGAASE GDFHAGLNMA AVLKCPVIFF CRNNGYAIST
PTEEQFAGNG IASRGVGYGM HTIRVDGNDM LAVLAATQQA RAYAIEHNAP VLIEAMTYRL
GAHSSSDDPS GYRSKDEEAK WQQHDPVKRF KLWLINKGWL AEADDVKLHE QYREEVLAAV
KVAEKLPVPM LDEIIEDVYD KPTPALKKQL SELKEHIKKY PQSYPKSAGR L
//
