Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q6ABX8 (ODPB_LEIXX)

Last modified November 4, 2008. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1
Gene names
Name: pdhB
Ordered Locus Names: Lxx25060
OrganismLeifsonia xyli subsp. xyli [Complete proteome] [HAMAP]
Taxonomic identifier59736 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

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.

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).

Cofactor

Thiamine pyrophosphate By similarity.

Subunit structure

Heterodimer of an alpha and a beta chain By similarity.

Ontologies

Keywords

   Biological processGlycolysis
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Pyruvate dehydrogenase E1 component subunit beta
PRO_0000232457

Sites

Binding site731Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6ABX8-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 2B45A895DC8D84E2

FASTA33736,087
        10         20         30         40         50         60 
MERAPALAEP EPRVQSLPMV KALNAGLRQA LVADPKVLIL GEDVGPLGGV FRVTEGLQSE 

        70         80         90        100        110        120 
FGASRVVDTP LAEAGIVGTA IGLAMRGYRP VVEIQFNGFV FPGFDQITTQ LAKMANRHSG 

       130        140        150        160        170        180 
AVSMPVVIRI PHGGHIGAVE HHQEAPEAYF AHTAGLRIVA PSTPHDAYWM IQEAIASDDP 

       190        200        210        220        230        240 
VIFFEPMSRY WPKGEVDTLE NPLPLHASRI VRSGTDATIV AWAGMVPVAL RAAEIAAEEG 

       250        260        270        280        290        300 
RSLEVVDLRS LAPIDYAPVL RSVQKTGRLV VAQEAPGIVS VGSEVAAVVG EKAFYSLEAP 

       310        320        330 
VLRVAGFDTP FPPAKLESLY LPDADRILEV VDRSLAY 

« Hide

Cross-references

Sequence databases

AE016822 Genomic DNA. Translation: AAT90114.1.
RefSeqYP_063219.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2940400.
GenomeReviewsGene locus Lxx25060 in contig AE016822_GR.
KEGGlxx:Lxx25060.
NMPDRfig|281090.3.peg.2006.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6ABX8.

Enzyme and pathway databases

BioCycLXYL281090:LXX25060-MON.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR005475. Transketo_Cen_R.
IPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_LEIXX
AccessionPrimary (citable) accession number: Q6ABX8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: September 13, 2004
Last modified: November 4, 2008
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information