ID G9A1B0_RHIFH Unreviewed; 410 AA.
AC G9A1B0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=bkdA1 {ECO:0000313|EMBL:CCE97490.1};
GN OrderedLocusNames=SFHH103_02998 {ECO:0000313|EMBL:CCE97490.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE97490.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE97490.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE97490.1,
RC ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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}.
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DR EMBL; HE616890; CCE97490.1; -; Genomic_DNA.
DR RefSeq; WP_014329898.1; NC_016812.1.
DR AlphaFoldDB; G9A1B0; -.
DR STRING; 1117943.SFHH103_02998; -.
DR GeneID; 48974631; -.
DR KEGG; sfh:SFHH103_02998; -.
DR PATRIC; fig|380.5.peg.3185; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_5; -.
DR Proteomes; UP000007735; Chromosome.
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; IPR022593; Oxoisoval_DH_suAlpha_N_dom.
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 Pfam; PF12573; OxoDH_E1alpha_N; 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 6..45
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 82..379
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45489 MW; 59A6EAC45EA6B7BC CRC64;
MDEFSRLSLH VPEPAVRPGD QPDFSNVKIP KAGSVPRPEV DVEPEAIRDL AYSIIRVLNR
EGEAVGPWAG LLSDEELLTG LRHMMLLRAF DARMLMAQRQ GKTSFYMQHL GEEAVSCAFR
RALRKGDMNF PTYRQAGLLI ADDYPMVDMM NQIFSNELDP CHGRQLPVMY TSKEHGFFTI
SGNLATQYVQ AVGWAMASAI KNDTRIAAGW IGDGSTAESD FHSSLVFAST YKAPVILNIV
NNQWAISTFQ GIARGGSGTF AARGLGFGIP ALRVDGNDYL AVYAVARWAA ERARRNLGPT
LIEYVTYRVG AHSTSDDPSA YRPKTESEAW PLGDPVLRLK KHLILRGAWS DERHAQAEAE
IMDQVIQAQK EAESHGTLHA GGRPSVRDIF EGVYAEMPPH IRRQRQKAGY
//
