ODPB_GEOSE
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 03-AUG-2022, entry version 114.
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; Firmicutes; 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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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;
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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 PRIDE; P21874; -.
DR GeneID; 58572154; -.
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 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; Direct protein sequencing; Glycolysis; Oxidoreductase;
KW Pyruvate; 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
