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Reviewed, UniProtKB/Swiss-Prot Q09171 (ODPB_SCHPO)

Last modified January 19, 2010. Version 75. 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

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Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
      Short name=PDHE1-B
    EC=1.2.4.1
Gene names
Name: pdb1
ORF Names: SPBC30D10.13c
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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).

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits.

Subcellular location

Mitochondrion matrix.

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Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   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

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 366Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020460

Sites

Binding site941Thiamine pyrophosphate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q09171-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5835A6872F6EDC0A

FASTA36639,624
        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

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References

« Hide 'large scale' references
[1]"Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta subunit of Schizosaccharomyces pombe."
Cavan G., Macdonald D.
Gene 152:117-120(1995) [PubMed: 7828917] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"The genome sequence of Schizosaccharomyces pombe."
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. expand/collapse author list , 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.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X75648 Genomic DNA. Translation: CAA53303.1.
CU329671 Genomic DNA. Translation: CAB10808.1.
PIRJC4080.
RefSeqNP_596272.1.

3D structure databases

SMRQ09171. Positions 37-365.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ09171.

Genome annotation databases

GeneID2540273.
GenomeReviewsGene locus pdb1 in contig CU329671_GR.
KEGGspo:SPBC30D10.13c.
NMPDRfig|4896.1.peg.2138.

Organism-specific databases

GeneDB_SpombeSPBC30D10.13c.

Phylogenomic databases

eggNOGfuNOG05078.
HOGENOMHBG753264.
OMAQDYAAWY.
OrthoDBEOG9X9908.
PhylomeDBQ09171.

Enzyme and pathway databases

BRENDA1.2.4.1. 653.

Gene expression databases

ArrayExpressQ09171.

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...

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Entry information

Entry nameODPB_SCHPO
AccessionPrimary (citable) accession number: Q09171
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 19, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

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