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UniProtKB/Swiss-Prot entry Q8HXW9


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

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Entry information
Entry name ODPA_MACFA
Primary accession number Q8HXW9
Secondary accession numbers None
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 33)
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
ORFNames: QccE-20080
From
Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) [TaxID: 9541] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
"Isolation and characterization of cDNA for macaque neurological disease genes.";
Submitted (APR-2002) 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
AB083322; BAC20601.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
SMR Q8HXW9; 29-390.
ModBase Q8HXW9.
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).
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 Q8HXW9.
Phylogenomic databases
HOVERGEN Q8HXW9; -.
Other
ProtoNet Q8HXW9.
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_0000020441
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: 43366 Da [This is the MW of the unprocessed precursor] CRC64: 420CE38364BDB33C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

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

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSTHMYAKNF YRGNGIVGAQ VPLGAGIALA 

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

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

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

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 

Q8HXW9 in FASTA format

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