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UniProtKB/Swiss-Prot entry P52904


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

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Entry information
Entry name ODPB_PEA
Primary accession number P52904
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 58)
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 None
From
Pisum sativum (Garden pea) [TaxID: 3888] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Luethy M.H., Miernyk J.A., Randall D.D.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
  • 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
U56697; AAB01223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T06532; T06532.
3D structure databases
HSSP P11177; 1NI4. [HSSP ENTRY / PDB]
ModBase P52904.
Protein-protein interaction databases
IntAct P52904; 1.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
Other
ProtoNet P52904.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
TRANSIT   1    19  19     Mitochondrion (By similarity). 
CHAIN   20   359  340     Pyruvate dehydrogenase E1 component subunit beta, mitochondrial. PRO_0000020463
BINDING   82    82        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 359 AA [This is the length of the unprocessed precursor] Molecular weight: 38793 Da [This is the MW of the unprocessed precursor] CRC64: 5AFE49F165C13C83 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG EEVGEYQGAY 

        70         80         90        100        110        120 
KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV VEFMTFNFSM QAIDHIINSA 

       130        140        150        160        170        180 
AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ HSHCYASWYG SCPGLKVLVP HSAEDARGLL 

       190        200        210        220        230        240 
KAAIRDPDPV VFLENELLYG ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG 

       250        260        270        280        290        300 
FALKAAEILE KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT 

       310        320        330        340        350 
SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH RSVPLAAAA 

P52904 in FASTA format

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View entry in raw text format (no links)
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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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