ID ODBB_THET2 Reviewed; 324 AA.
AC Q72GU2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE Short=BCKDH E1-beta;
GN OrderedLocusNames=TT_C1756;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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) (By similarity).
CC {ECO:0000250|UniProtKB:P37941}.
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:0000250|UniProtKB:Q5SLR3};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q5SLR3};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly
CC associated with ODBA in the E1 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q5SLR3}.
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DR EMBL; AE017221; AAS82098.1; -; Genomic_DNA.
DR RefSeq; WP_011174114.1; NZ_CP133179.1.
DR AlphaFoldDB; Q72GU2; -.
DR SMR; Q72GU2; -.
DR KEGG; tth:TT_C1756; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_0; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..324
FT /note="2-oxoisovalerate dehydrogenase subunit beta"
FT /id="PRO_0000294976"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5SLR3, ECO:0000305"
FT BINDING 29
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q5SLR3"
FT BINDING 58..60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:Q5SLR3"
FT BINDING 83..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86..89
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SLR3"
SQ SEQUENCE 324 AA; 35083 MW; 6799254F5589D04A CRC64;
MALMTMVQAL NRALDEEMAK DPRVVVLGED VGKRGGVFLV TEGLLQKYGP DRVMDTPLSE
AAIVGAALGM AAHGLRPVAE IQFADYIFPG FDQLVSQVAK LRYRSGGQFT APLVVRMPSG
GGVRGGHHHS QSPEAHFVHT AGLKVVAVST PYDAKGLLKA AIRDEDPVVF LEPKRLYRSV
KEEVPEEDYT LSIGKAALRR EGKDLTLIGY GTVMPEVLQA AAELAKAGVS AEVLDLRTLM
PWDYEAVMNS VAKTGRVVLV SDAPRHASFV SEVAATIAED LLDMLLAPPI RVTGFDTPYP
YAQDKLYLPT VTRILNAAKR ALDY
//
