ID ODPB_GEOSE Reviewed; 325 AA. AC P21874; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 122. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta; DE EC=1.2.4.1; GN Name=pdhB; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924; RX PubMed=2200674; DOI=10.1111/j.1432-1033.1990.tb19128.x; RA Hawkins C.F., Borges A., Perham R.N.; RT "Cloning and sequence analysis of the genes encoding the alpha and beta RT subunits of the E1 component of the pyruvate dehydrogenase multienzyme RT complex of Bacillus stearothermophilus."; RL Eur. J. Biochem. 191:337-346(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2253629; DOI=10.1111/j.1432-1033.1990.tb19432.x; RA Borges A., Hawkins C.F., Packman L.C., Perham R.N.; RT "Cloning and sequence analysis of the genes encoding the dihydrolipoamide RT acetyltransferase and dihydrolipoamide dehydrogenase components of the RT pyruvate dehydrogenase multienzyme complex of Bacillus RT stearothermophilus."; RL Eur. J. Biochem. 194:95-102(1990). CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple CC copies of three enzymatic components: pyruvate dehydrogenase (E1), CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase CC (E3). CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)- CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. CC -!- INTERACTION: CC P21874; P21873: pdhA; NbExp=3; IntAct=EBI-1040700, EBI-1040686; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X53560; CAA37629.1; -; Genomic_DNA. DR PIR; S14230; S14230. DR RefSeq; WP_033016213.1; NZ_RCTK01000001.1. DR PDB; 1W85; X-ray; 2.00 A; B/D/F/H=2-325. DR PDB; 1W88; X-ray; 2.30 A; B/D/F/H=2-325. DR PDB; 3DUF; X-ray; 2.50 A; B/D/F/H=1-325. DR PDB; 3DV0; X-ray; 2.50 A; B/D/F/H=1-325. DR PDB; 3DVA; X-ray; 2.35 A; B/D/F/H=1-325. DR PDBsum; 1W85; -. DR PDBsum; 1W88; -. DR PDBsum; 3DUF; -. DR PDBsum; 3DV0; -. DR PDBsum; 3DVA; -. DR AlphaFoldDB; P21874; -. DR SMR; P21874; -. DR DIP; DIP-29597N; -. DR IntAct; P21874; 2. DR GeneID; 69834553; -. DR OrthoDB; 9771835at2; -. DR BRENDA; 1.2.4.1; 623. DR SABIO-RK; P21874; -. DR EvolutionaryTrace; P21874; -. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. 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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1. DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Oxidoreductase; Pyruvate; KW Thiamine pyrophosphate. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..325 FT /note="Pyruvate dehydrogenase E1 component subunit beta" FT /id="PRO_0000162221" FT BINDING 60 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /evidence="ECO:0000250" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1W88" FT HELIX 6..20 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:3DUF" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 44..48 FT /evidence="ECO:0007829|PDB:1W85" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 60..72 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 84..89 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:1W85" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:1W85" FT TURN 127..129 FT /evidence="ECO:0007829|PDB:1W88" FT HELIX 134..137 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:1W85" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:1W88" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 203..209 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 213..226 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 244..254 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 257..264 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 270..281 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:1W85" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 305..308 FT /evidence="ECO:0007829|PDB:1W85" FT HELIX 312..323 FT /evidence="ECO:0007829|PDB:1W85" SQ SEQUENCE 325 AA; 35460 MW; AD1F2D4F82D652AC CRC64; MAQMTMVQAI TDALRIELKN DPNVLIFGED VGVNGGVFRA TEGLQAEFGE DRVFDTPLAE SGIGGLAIGL ALQGFRPVPE IQFFGFVYEV MDSICGQMAR IRYRTGGRYH MPITIRSPFG GGVHTPELHS DSLEGLVAQQ PGLKVVIPST PYDAKGLLIS AIRDNDPVIF LEHLKLYRSF RQEVPEGEYT IPIGKADIKR EGKDITIIAY GAMVHESLKA AAELEKEGIS AEVVDLRTVQ PLDIETIIGS VEKTGRAIVV QEAQRQAGIA ANVVAEINER AILSLEAPVL RVAAPDTVYP FAQAESVWLP NFKDVIETAK KVMNF //