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UniProtKB/Swiss-Prot entry Q09171


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

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Entry information
Entry name ODPB_SCHPO
Primary accession number Q09171
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta, mitochondrial [Precursor]
Synonyms PDHE1-B
EC 1.2.4.1
Gene name
Name: pdb1
ORFNames: SPBC30D10.13c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1016/0378-1119(94)00705-W; PubMed=7828917 [NCBI, ExPASy, EBI, Israel, Japan]
Cavan G., Macdonald D.;
"Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta subunit of Schizosaccharomyces pombe.";
Gene 152:117-120(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
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).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
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
X75648; CAA53303.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAB10808.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4080; JC4080.
RefSeq NP_596272.1; -.
3D structure databases
HSSP P11177; 1NI4. [HSSP ENTRY / PDB]
ModBase Q09171.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004295-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC30D10.13c; -.
Gene expression databases
ArrayExpress Q09171; -.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from GeneDB_SPombe).
QuickGo view.
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 Q09171.
Genome annotation databases
GeneID 2540273; -.
KEGG spo:SPBC30D10.13c; -.
NMPDR fig|4896.1.peg.2138; -.
Other
ProtoNet Q09171.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1     ?        Mitochondrion (Potential). 
CHAIN   ?   366        Pyruvate dehydrogenase E1 component subunit beta, mitochondrial. PRO_0000020460
BINDING   94    94        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 366 AA [This is the length of the unprocessed precursor] Molecular weight: 39624 Da [This is the MW of the unprocessed precursor] CRC64: 5835A6872F6EDC0A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIRLQKFGEI VGTSRSWKLL SSTIAKRYSS SSNGVKEMTV RDALNSAMEE EMKRDDRVFL 

        70         80         90        100        110        120 
IGEEVAQYNG AYKISRGLLD KFGPKRVIDT PITEMGFTGL ATGAAFAGLR PICEFMTFNF 

       130        140        150        160        170        180 
SMQAIDHIVN SAARTLYMSG GIQACPIVFR GPNGPAAAVA AQHSQHFAPW YGSIPGLKVV 

       190        200        210        220        230        240 
SPYSAEDARG LLKAAIRDPN PVVVLENEIL YGKTFPISKE ALSEDFVLPF GLAKVERPGK 

       250        260        270        280        290        300 
DITIVGESIS VVTALEAADK LKADYGVEAE VINLRSIRPL DINTIAASVK KTNRIVTVDQ 

       310        320        330        340        350        360 
AYSQHGIGSE IAAQIMESDA FDYLDAPVER VSMADVPMPY SHPVEAASVP NADVVVAAAK 


KCLYIK 

Q09171 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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