ID L0KEC0_MESAW Unreviewed; 410 AA.
AC L0KEC0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 OrderedLocusNames=Mesau_00862 {ECO:0000313|EMBL:AGB43346.1};
OS Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB43346.1, ECO:0000313|Proteomes:UP000010998};
RN [1] {ECO:0000313|Proteomes:UP000010998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC {ECO:0000313|Proteomes:UP000010998};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT "Complete sequence of Mesorhizobium australicum WSM2073.";
RL Submitted (FEB-2012) 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|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; CP003358; AGB43346.1; -; Genomic_DNA.
DR RefSeq; WP_015314818.1; NC_019973.1.
DR AlphaFoldDB; L0KEC0; -.
DR STRING; 754035.Mesau_00862; -.
DR KEGG; mam:Mesau_00862; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_5; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000010998; 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}; Pyruvate {ECO:0000313|EMBL:AGB43346.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010998};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 7..44
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 83..379
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 44655 MW; 19B5FCB026B09A0E CRC64;
MADAGMLRFH VPEPEVRPGG TPDFSNVTIA EAGSVPRPDI DVDPRTIRDM AFSIIRVLNR
NGEAVGPWAG LLSSEELLEG LRNMMTLRTF DARMQMAQRQ GKTSFYMQHL GEEAVSCAFR
KALAPGDMNF PTYRQAGLLI ADGYPMVTMM NQIYSNEADP LKGRQLPIMY SSKEHGFFSI
SGNLATQYIQ AVGWAMASAI SNDSRIAAAW IGDGSTAESD FHSALVFAST YKAPVVLNVV
NNQWAISTFQ GIARGGSGTF AARGLGFGIP SLRVDGNDYL AVHAVAKWAA TRARDNLGPT
LVEYVTYRAG AHSSSDDPSA YRPKTESDAW PLGDPVVRLK NHLIKLGVWS DERHAQAEAE
ILDTVIAAQK EAESHGTLHA GGKPSTREMF EGVFAEMPPH LRRQRQQAGV
//