Reviewed, UniProtKB/Swiss-Prot P26284 (ODPA_RAT)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
    EC=1.2.4.1
Alternative name(s):
    PDHE1-A type I

Gene names

Name:

Pdha1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits.
Subcellular location	Mitochondrion matrix.
Tissue specificity	In all tissues, but in very low amount in testis.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay. Source: RGD glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial pyruvate dehydrogenase complex Ref.2 Traceable author statement. Source: RGD
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Ref.2 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion By similarity
	Chain	30 – 390	361	Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial		PRO_0000020445
Amino acid modifications
	Modified residue	232	1	Phosphoserine By similarity
	Modified residue	289	1	Phosphotyrosine By similarity
	Modified residue	293	1	Phosphoserine Ref.4
	Modified residue	295	1	Phosphoserine Ref.4
	Modified residue	300	1	Phosphoserine Ref.4
	Modified residue	301	1	Phosphotyrosine Ref.4
Experimental info
	Sequence conflict	10	1	R → H in CAA78146. Ref.2
	Sequence conflict	126	1	N → T in CAA78146. Ref.2
	Sequence conflict	129 – 130	2	HA → LP in CAA78146. Ref.2
	Sequence conflict	134	1	I → V Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P26284-1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 254B5A801E750DC0	FASTA	390	43,227
	10 20 30 40 50 60 MRKMLAAVSR VLAGAAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 130 140 150 160 170 180 HGFTFNRGHA VRAILAELTG 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 LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase." Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T. Biochim. Biophys. Acta 1089:1-7(1991) [PubMed: 2025639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The pyruvate dehydrogenase complex: cloning of the rat somatic E1 alpha subunit and its coordinate expression with the mRNAs for the E1 beta, E2, and E3 catalytic subunits in developing rat brain." Cullingford T.E., Clark J.B., Phillips I.R. J. Neurochem. 62:1682-1690(1994) [PubMed: 8158120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	Lubec G., Diao W., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 133-141; 216-226; 245-253; 289-302 AND 324-343, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[4]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295; SER-300 AND TYR-301, MASS SPECTROMETRY. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z12158 mRNA. Translation: CAA78146.1.
IPI	IPI00191707.
PIR	DERTPA. S15891. DERTP1. S21553.
UniGene	Rn.3655
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	P26284. Positions 29-390.
ModBase	Search...
PTM databases
PhosphoSite	P26284.
Proteomic databases
PRIDE	P26284.
Genome annotation databases
Ensembl	ENSRNOG00000025383. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	3286. Pdha1.
Phylogenomic databases
HOVERGEN	P26284.
Enzyme and pathway databases
BRENDA	1.2.4.1. 248.
Gene expression databases
ArrayExpress	P26284.
GermOnline	ENSRNOG00000025383. Rattus norvegicus.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_RAT

Accession

Primary (citable) accession number: P26284

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 12, 2006
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)