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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

pdb1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein predictedi

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: PomBase

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: PomBase
  2. arginine biosynthetic process Source: PomBase
  3. glutamine biosynthetic process Source: PomBase
  4. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_332635. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_341792. Pyruvate metabolism.
REACT_352376. Signaling by Retinoic Acid.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-B
Gene namesi
Name:pdb1
ORF Names:SPBC30D10.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

PomBaseiSPBC30D10.13c.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial pyruvate dehydrogenase complex Source: PomBase
  2. mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 366Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020460
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ09171.
PaxDbiQ09171.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits.

Protein-protein interaction databases

BioGridi276804. 5 interactions.
MINTiMINT-4693703.
STRINGi4896.SPBC30D10.13c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09171.
SMRiQ09171. Positions 37-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
HOGENOMiHOG000281450.
InParanoidiQ09171.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7GBG70.
PhylomeDBiQ09171.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q09171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRLQKFGEI VGTSRSWKLL SSTIAKRYSS SSNGVKEMTV RDALNSAMEE
60 70 80 90 100
EMKRDDRVFL IGEEVAQYNG AYKISRGLLD KFGPKRVIDT PITEMGFTGL
110 120 130 140 150
ATGAAFAGLR PICEFMTFNF SMQAIDHIVN SAARTLYMSG GIQACPIVFR
160 170 180 190 200
GPNGPAAAVA AQHSQHFAPW YGSIPGLKVV SPYSAEDARG LLKAAIRDPN
210 220 230 240 250
PVVVLENEIL YGKTFPISKE ALSEDFVLPF GLAKVERPGK DITIVGESIS
260 270 280 290 300
VVTALEAADK LKADYGVEAE VINLRSIRPL DINTIAASVK KTNRIVTVDQ
310 320 330 340 350
AYSQHGIGSE IAAQIMESDA FDYLDAPVER VSMADVPMPY SHPVEAASVP
360
NADVVVAAAK KCLYIK
Length:366
Mass (Da):39,624
Last modified:November 1, 1995 - v1
Checksum:i5835A6872F6EDC0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75648 Genomic DNA. Translation: CAA53303.1.
CU329671 Genomic DNA. Translation: CAB10808.1.
PIRiJC4080.
RefSeqiNP_596272.1. NM_001022193.2.

Genome annotation databases

EnsemblFungiiSPBC30D10.13c.1; SPBC30D10.13c.1:pep; SPBC30D10.13c.
GeneIDi2540273.
KEGGispo:SPBC30D10.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75648 Genomic DNA. Translation: CAA53303.1.
CU329671 Genomic DNA. Translation: CAB10808.1.
PIRiJC4080.
RefSeqiNP_596272.1. NM_001022193.2.

3D structure databases

ProteinModelPortaliQ09171.
SMRiQ09171. Positions 37-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276804. 5 interactions.
MINTiMINT-4693703.
STRINGi4896.SPBC30D10.13c-1.

Proteomic databases

MaxQBiQ09171.
PaxDbiQ09171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC30D10.13c.1; SPBC30D10.13c.1:pep; SPBC30D10.13c.
GeneIDi2540273.
KEGGispo:SPBC30D10.13c.

Organism-specific databases

PomBaseiSPBC30D10.13c.

Phylogenomic databases

eggNOGiCOG0022.
HOGENOMiHOG000281450.
InParanoidiQ09171.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7GBG70.
PhylomeDBiQ09171.

Enzyme and pathway databases

ReactomeiREACT_332635. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_341792. Pyruvate metabolism.
REACT_352376. Signaling by Retinoic Acid.

Miscellaneous databases

NextBioi20801403.
PROiQ09171.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  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.
    , 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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiODPB_SCHPO
AccessioniPrimary (citable) accession number: Q09171
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 1, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.