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Protein

Pyruvate dehydrogenase E1 component subunit beta

Gene

pdhB

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63Thiamine pyrophosphateBy similarity1

GO - Molecular functioni

  • fibronectin binding Source: CAFA
  • pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  • catabolism by symbiont of host protein Source: AgBase
  • glycolytic process Source: UniProtKB-KW
  • interaction with host via substance in symbiont cell outer membrane Source: CAFA
  • plasminogen activation Source: AgBase
  • positive regulation of fibrinolysis Source: AgBase

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandPyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-587.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta (EC:1.2.4.1)
Gene namesi
Name:pdhB
Ordered Locus Names:MPN_392
ORF Names:MP446
OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
Taxonomic identifieri272634 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
Proteomesi
  • UP000000808 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • attachment organelle membrane Source: CAFA
  • cell surface Source: AgBase
  • cytosol Source: AgBase
  • external side of plasma membrane Source: CAFA
  • membrane Source: AgBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622241 – 327Pyruvate dehydrogenase E1 component subunit betaAdd BLAST327

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PLGP0074711EBI-2259621,EBI-999394From Homo sapiens.

GO - Molecular functioni

  • fibronectin binding Source: CAFA

Protein-protein interaction databases

IntActiP75391. 5 interactors.

Structurei

3D structure databases

ProteinModelPortaliP75391.
SMRiP75391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

KOiK00162.
OMAiDTKGLML.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
InterProiView protein in InterPro
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
PfamiView protein in Pfam
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
SMARTiView protein in SMART
SM00861. Transket_pyr. 1 hit.
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

P75391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTIQANNI EALGNAMDLA LERDPNVVLY GQDAGFEGGV FRATKGLQKK
60 70 80 90 100
YGEERVWDCP IAEAAMAGIG VGAAIGGLKP IVEIQFSGFS FPAMFQIFTH
110 120 130 140 150
AARIRNRSRG VYTCPIIVRM PMGGGIKALE HHSETLEAIY GQIAGLKTVM
160 170 180 190 200
PSNPYDTKGL FLAAVESPDP VVFFEPKKLY RAFRQEIPAD YYTVPIGQAN
210 220 230 240 250
LISQGNNLTI VSYGPTMFDL INMVYGGELK DKGIELIDLR TISPWDKETV
260 270 280 290 300
FNSVKKTGRL LVVTEAAKTF TTSGEIIASV TEELFSYLKA APQRVTGWDI
310 320
VVPLARGEHY QFNLNARILE AVNQLLK
Length:327
Mass (Da):35,914
Last modified:February 1, 1997 - v1
Checksum:i06513520FDAFED54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96094.1.
PIRiS73772.
RefSeqiNP_110080.1. NC_000912.1.
WP_010874748.1. NC_000912.1.

Genome annotation databases

EnsemblBacteriaiAAB96094; AAB96094; MPN_392.
GeneIDi877125.
KEGGimpn:MPN392.
PATRICi20022160. VBIMycPne110_0423.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA. Translation: AAB96094.1.
PIRiS73772.
RefSeqiNP_110080.1. NC_000912.1.
WP_010874748.1. NC_000912.1.

3D structure databases

ProteinModelPortaliP75391.
SMRiP75391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP75391. 5 interactors.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB96094; AAB96094; MPN_392.
GeneIDi877125.
KEGGimpn:MPN392.
PATRICi20022160. VBIMycPne110_0423.

Phylogenomic databases

KOiK00162.
OMAiDTKGLML.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-587.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
InterProiView protein in InterPro
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
PfamiView protein in Pfam
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
SMARTiView protein in SMART
SM00861. Transket_pyr. 1 hit.
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiODPB_MYCPN
AccessioniPrimary (citable) accession number: P75391
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 10, 2017
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Mycoplasma pneumoniae
    Mycoplasma pneumoniae (strain M129): entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.