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UniProtKB/Swiss-Prot entry P75391


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPB_MYCPN
Primary accession number P75391
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 51)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta
Synonym EC 1.2.4.1
Gene name
Name: pdhB
OrderedLocusNames: MPN_392
ORFNames: MP446
From
Mycoplasma pneumoniae [TaxID: 2104] [HAMAP proteome]
Taxonomy Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
DOI=10.1093/nar/24.22.4420; PubMed=8948633 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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 + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00089; AAB96094.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S73772; S73772.
RefSeq NP_110080.1; -.
3D structure databases
HSSP Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]
ModBase P75391.
Enzyme and pathway databases
BioCyc MetaCyc:MON-587; -.
MPNE272634:MPN392-MON; -.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS P75391.
Genome annotation databases
GeneID 877125; -.
GenomeReviews U00089_GR; MPN_392.
KEGG mpn:MPN392; -.
Phylogenomic databases
HOGENOM P75391; -.
Genome annotation databases
CMR P75391; MPN_392.
Other
ProtoNet P75391.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   327  327     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000162224
BINDING   63    63        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 327 AA [This is the length of the unprocessed precursor] Molecular weight: 35914 Da [This is the MW of the unprocessed precursor] CRC64: 06513520FDAFED54 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKTIQANNI EALGNAMDLA LERDPNVVLY GQDAGFEGGV FRATKGLQKK YGEERVWDCP 

        70         80         90        100        110        120 
IAEAAMAGIG VGAAIGGLKP IVEIQFSGFS FPAMFQIFTH AARIRNRSRG VYTCPIIVRM 

       130        140        150        160        170        180 
PMGGGIKALE HHSETLEAIY GQIAGLKTVM PSNPYDTKGL FLAAVESPDP VVFFEPKKLY 

       190        200        210        220        230        240 
RAFRQEIPAD YYTVPIGQAN LISQGNNLTI VSYGPTMFDL INMVYGGELK DKGIELIDLR 

       250        260        270        280        290        300 
TISPWDKETV FNSVKKTGRL LVVTEAAKTF TTSGEIIASV TEELFSYLKA APQRVTGWDI 

       310        320 
VVPLARGEHY QFNLNARILE AVNQLLK 

P75391 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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