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Reviewed, UniProtKB/Swiss-Prot P47515 (ODPB_MYCGE)

Last modified January 19, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1
Gene names
Name: pdhB
Ordered Locus Names: MG273
OrganismMycoplasma genitalium [Complete proteome] [HAMAP]
Taxonomic identifier2097 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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.

Catalytic activity

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

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 – 326326Pyruvate dehydrogenase E1 component subunit beta
PRO_0000162223

Sites

Binding site621Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P47515-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7C5A0ECCD8A17DD7

FASTA32636,026
        10         20         30         40         50         60 
MSKIQVNNIE ALNNAMDLAL ERDQNVVLYG QDAGFEGGVF RATKGLQQKY GSERVWDCPI 

        70         80         90        100        110        120 
AENSMAGIGV GAAIGGLKPI VEIQFSGFSF PAMFQIFVHA ARIRNRSRGV YTAPLVVRMP 

       130        140        150        160        170        180 
MGGGIKALEH HSETLEAIYA QIAGLKTVMP SNPYDTKGLF LAAIESPDPV IFFEPKKLYR 

       190        200        210        220        230        240 
AFRQEIPSDY YTVPIGEANL ISEGSELTIV SYGPTMFDLI NLVYSGELKD KGIELIDLRT 

       250        260        270        280        290        300 
ISPWDKQTVF NSVKKTGRLL VVTEAVKSFT TSAEIITSVT EELFTYLKKA PQRVTGFDIV 

       310        320 
VPLARGEKYQ FEINARVIDA VNQLLK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43967 Genomic DNA. Translation: AAC71495.1.
PIRB64230.
RefSeqNP_072940.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID875399.
GenomeReviewsGene locus MG273 in contig L43967_GR.
KEGGmge:MG_273.
TIGRMG273.

Phylogenomic databases

HOGENOMHBG753264.
OMALEHHSET.

Enzyme and pathway databases

BioCycMGEN243273:MG_273-MONOMER.
BRENDA1.2.4.1. 110.

Family and domain databases

InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_MYCGE
AccessionPrimary (citable) accession number: P47515
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 19, 2010
This is version 59 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)

Relevant documents

Mycoplasma genitalium

Mycoplasma genitalium (strain G-37): entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents