ODBB_THET8
ID ODBB_THET8 Reviewed; 324 AA.
AC Q5SLR3; P84130;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=TTHA0230;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1] {ECO:0000312|EMBL:BAD70053.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|PDB:1UM9}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBA AND THIAMINE
RP PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=15033367; DOI=10.1016/j.jmb.2004.02.011;
RA Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N.;
RT "Ligand-induced conformational changes and a reaction intermediate in
RT branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8,
RT as revealed by X-ray crystallography.";
RL J. Mol. Biol. 337:1011-1033(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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
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:0000269|PubMed:15033367, ECO:0000305};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:15033367, ECO:0000305};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly
CC associated with ODBA in the E1 complex. {ECO:0000269|PubMed:15033367,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q5SLR3; Q5SLR4: TTHA0229; NbExp=4; IntAct=EBI-1038230, EBI-1038222;
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DR EMBL; AP008226; BAD70053.1; -; Genomic_DNA.
DR RefSeq; WP_011227794.1; NC_006461.1.
DR RefSeq; YP_143496.1; NC_006461.1.
DR PDB; 1UM9; X-ray; 2.20 A; B/D=1-324.
DR PDB; 1UMB; X-ray; 2.10 A; B/D=1-324.
DR PDB; 1UMC; X-ray; 2.40 A; B/D=1-324.
DR PDB; 1UMD; X-ray; 1.90 A; B/D=1-324.
DR PDBsum; 1UM9; -.
DR PDBsum; 1UMB; -.
DR PDBsum; 1UMC; -.
DR PDBsum; 1UMD; -.
DR AlphaFoldDB; Q5SLR3; -.
DR SMR; Q5SLR3; -.
DR IntAct; Q5SLR3; 1.
DR STRING; 300852.55771612; -.
DR EnsemblBacteria; BAD70053; BAD70053; BAD70053.
DR GeneID; 3168889; -.
DR KEGG; ttj:TTHA0230; -.
DR PATRIC; fig|300852.9.peg.228; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_0_0; -.
DR OMA; SEAYYMA; -.
DR PhylomeDB; Q5SLR3; -.
DR EvolutionaryTrace; Q5SLR3; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.920; -; 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 Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..324
FT /note="2-oxoisovalerate dehydrogenase subunit beta"
FT /id="PRO_0000294977"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 29
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:15033367"
FT BINDING 58..60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 82
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:15033367"
FT BINDING 83..86
FT /ligand="substrate"
FT BINDING 86..89
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1UMD"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:1UMD"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:1UMD"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1UMD"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1UMD"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1UMD"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:1UMD"
SQ SEQUENCE 324 AA; 35093 MW; 679926805496D29A CRC64;
MALMTMVQAL NRALDEEMAK DPRVVVLGED VGKRGGVFLV TEGLLQKYGP DRVMDTPLSE
AAIVGAALGM AAHGLRPVAE IQFADYIFPG FDQLVSQVAK LRYRSGGQFT APLVVRMPSG
GGVRGGHHHS QSPEAHFVHT AGLKVVAVST PYDAKGLLKA AIRDEDPVVF LEPKRLYRSV
KEEVPEEDYT LPIGKAALRR EGKDLTLIGY GTVMPEVLQA AAELAKAGVS AEVLDLRTLM
PWDYEAVMNS VAKTGRVVLV SDAPRHASFV SEVAATIAED LLDMLLAPPI RVTGFDTPYP
YAQDKLYLPT VTRILNAAKR ALDY
