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UniProtKB/Swiss-Prot entry P47515


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

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Entry information
Entry name ODPB_MYCGE
Primary accession number P47515
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 50)
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: MG273
From
Mycoplasma genitalium [TaxID: 2097] [HAMAP proteome]
Taxonomy Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33530 / G-37 / NCTC 10195;
PubMed=7569993 [NCBI, ExPASy, EBI, Israel, Japan]
Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
"The minimal gene complement of Mycoplasma genitalium.";
Science 270:397-403(1995).
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
L43967; AAC71495.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B64230; B64230.
RefSeq NP_072940.1; -.
3D structure databases
HSSP Q8ZUR7; 1IK6. [HSSP ENTRY / PDB]
ModBase P47515.
Enzyme and pathway databases
BioCyc MGEN243273:MG_273-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 P47515.
Genome annotation databases
GeneID 875399; -.
GenomeReviews L43967_GR; MG273.
KEGG mge:MG_273; -.
TIGR MG273; -.
Phylogenomic databases
HOGENOM P47515; -.
Other
ProtoNet P47515.
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   326  326     Pyruvate dehydrogenase E1 component subunit beta. PRO_0000162223
BINDING   62    62        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 36026 Da [This is the MW of the unprocessed precursor] CRC64: 7C5A0ECCD8A17DD7 [This is a checksum on the sequence]
        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 

P47515 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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