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Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1)

 ODPB_MYCPN              Reviewed;         327 AA.
P75391;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-JUN-2017, entry version 101.
RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
EC=1.2.4.1;
Name=pdhB; OrderedLocusNames=MPN_392; ORFNames=MP446;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
-!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
conversion of pyruvate to acetyl-CoA and CO(2). It contains
multiple copies of three enzymatic components: pyruvate
dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000250};
-!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
-!- INTERACTION:
P02788:LTF (xeno); NbExp=3; IntAct=EBI-2259621, EBI-1058602;
P00747:PLG (xeno); NbExp=11; IntAct=EBI-2259621, EBI-999394;
P04004:VTN (xeno); NbExp=3; IntAct=EBI-2259621, EBI-1036653;
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EMBL; U00089; AAB96094.1; -; Genomic_DNA.
PIR; S73772; S73772.
RefSeq; NP_110080.1; NC_000912.1.
RefSeq; WP_010874748.1; NC_000912.1.
ProteinModelPortal; P75391; -.
SMR; P75391; -.
IntAct; P75391; 7.
EnsemblBacteria; AAB96094; AAB96094; MPN_392.
GeneID; 877125; -.
KEGG; mpn:MPN392; -.
PATRIC; fig|272634.6.peg.423; -.
KO; K00162; -.
OMA; VQERCFH; -.
BioCyc; MetaCyc:MONOMER-587; -.
Proteomes; UP000000808; Chromosome.
GO; GO:0033111; C:attachment organelle membrane; IDA:CAFA.
GO; GO:0009986; C:cell surface; IDA:AgBase.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
GO; GO:0052014; P:catabolism by symbiont of host protein; IDA:AgBase.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
GO; GO:0044045; P:interaction with host via substance in symbiont cell outer membrane; IMP:CAFA.
GO; GO:0031639; P:plasminogen activation; IDA:AgBase.
GO; GO:0051919; P:positive regulation of fibrinolysis; IDA:AgBase.
Gene3D; 3.40.50.920; -; 1.
InterPro; IPR029061; THDP-binding.
InterPro; IPR009014; Transketo_C/PFOR_II.
InterPro; IPR005475; Transketolase-like_Pyr-bd.
InterPro; IPR033248; Transketolase_C.
Pfam; PF02779; Transket_pyr; 1.
Pfam; PF02780; Transketolase_C; 1.
SMART; SM00861; Transket_pyr; 1.
SUPFAM; SSF52518; SSF52518; 1.
SUPFAM; SSF52922; SSF52922; 1.
1: Evidence at protein level;
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
Reference proteome; Thiamine pyrophosphate.
CHAIN 1 327 Pyruvate dehydrogenase E1 component
subunit beta.
/FTId=PRO_0000162224.
BINDING 63 63 Thiamine pyrophosphate. {ECO:0000250}.
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


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