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UniProtKB/Swiss-Prot entry A7MB35


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

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Entry information
Entry name ODPA_BOVIN
Primary accession number A7MB35
Secondary accession numbers None
Integrated into Swiss-Prot on April 8, 2008
Sequence was last modified on October 2, 2007 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 10)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial [Precursor]
Synonyms EC 1.2.4.1
PDHE1-A type I
Gene name
Name: PDHA1
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Hypothalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUL-2007) 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) (By similarity).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit (By similarity).
  • SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
  • SUBCELLULAR LOCATION: Mitochondrion matrix (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
BC151313; AAI51314.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001094516.1; -.
UniGene Bt.19415
3D structure databases
ModBase A7MB35.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS A7MB35.
Genome annotation databases
Ensembl ENSBTAG00000019852; Bos taurus. [Contig view]
GeneID 407109; -.
KEGG bta:407109; -.
Other
ProtoNet A7MB35.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    29  29     Mitochondrion (By similarity). 
CHAIN   30   390  361     Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial. PRO_0000329312
MOD_RES   232   232        Phosphoserine (By similarity). 
MOD_RES   289   289        Phosphotyrosine (By similarity). 
MOD_RES   293   293        Phosphoserine (By similarity). 
MOD_RES   295   295        Phosphoserine (By similarity). 
MOD_RES   300   300        Phosphoserine (By similarity). 
MOD_RES   301   301        Phosphotyrosine (By similarity). 
Sequence information
Length: 390 AA [This is the length of the unprocessed precursor] Molecular weight: 43388 Da [This is the MW of the unprocessed precursor] CRC64: 1297C2B1960BBEDF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKMLAAVSR VLSGVAQKPA SRVLVASRHF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYC NDPPFEVRGA NQWIKFKSIS 

A7MB35 in FASTA format

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