ID   ODPB_MYCPN              Reviewed;         327 AA.
AC   P75391;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; OrderedLocusNames=MPN_392; ORFNames=MP446;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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) (By similarity). {ECO:0000250}.
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         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P75391; P02788: LTF; Xeno; NbExp=3; IntAct=EBI-2259621, EBI-1058602;
CC       P75391; P00747: PLG; Xeno; NbExp=11; IntAct=EBI-2259621, EBI-999394;
CC       P75391; P04004: VTN; Xeno; NbExp=3; IntAct=EBI-2259621, EBI-1036653;
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DR   EMBL; U00089; AAB96094.1; -; Genomic_DNA.
DR   PIR; S73772; S73772.
DR   RefSeq; NP_110080.1; NC_000912.1.
DR   RefSeq; WP_010874748.1; NC_000912.1.
DR   AlphaFoldDB; P75391; -.
DR   SMR; P75391; -.
DR   IntAct; P75391; 7.
DR   STRING; 272634.MPN_392; -.
DR   MoonProt; P75391; -.
DR   EnsemblBacteria; AAB96094; AAB96094; MPN_392.
DR   GeneID; 66608949; -.
DR   KEGG; mpn:MPN_392; -.
DR   PATRIC; fig|272634.6.peg.423; -.
DR   HOGENOM; CLU_012907_1_0_14; -.
DR   OMA; SEAYYMA; -.
DR   BioCyc; MetaCyc:MON-587; -.
DR   BioCyc; MPNE272634:G1GJ3-622-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0033111; C:attachment organelle membrane; IDA:CAFA.
DR   GO; GO:0009986; C:cell surface; IDA:AgBase.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
DR   GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0031639; P:plasminogen activation; IDA:AgBase.
DR   GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase.
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   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..327
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000162224"
FT   BINDING         63
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  35914 MW;  06513520FDAFED54 CRC64;
     MSKTIQANNI EALGNAMDLA LERDPNVVLY GQDAGFEGGV FRATKGLQKK YGEERVWDCP
     IAEAAMAGIG VGAAIGGLKP IVEIQFSGFS FPAMFQIFTH AARIRNRSRG VYTCPIIVRM
     PMGGGIKALE HHSETLEAIY GQIAGLKTVM PSNPYDTKGL FLAAVESPDP VVFFEPKKLY
     RAFRQEIPAD YYTVPIGQAN LISQGNNLTI VSYGPTMFDL INMVYGGELK DKGIELIDLR
     TISPWDKETV FNSVKKTGRL LVVTEAAKTF TTSGEIIASV TEELFSYLKA APQRVTGWDI
     VVPLARGEHY QFNLNARILE AVNQLLK