Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial precursor

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Q06437 (ODPAT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
EC=1.2.4.1

Alternative name(s):
PDHE1-A type II

Gene names

Name:

Pdha2

Organism

Rattus norvegicus (Rat) [Reference proteome]

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	391 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, and thereby links the glycolytic pathway to the tricarboxylic cycle. Ref.2
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂. Ref.2
Cofactor	Thiamine pyrophosphate By similarity.
Enzyme regulation	Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation By similarity.
Subunit structure	Heterotetramer of two PDHA2 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Tissue specificity	Testis. Ref.2

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7487891. Source: RGD glycolysis Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 7487891. Source: RGD pyruvate dehydrogenase complex Inferred from direct assay PubMed 7487891. Source: RGD
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from direct assay PubMed 7487891. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion By similarity

Chain

31 – 391

361

Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial

PRO_0000020449

Amino acid modifications

Modified residue

294

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 By similarity

Modified residue

301

Phosphoserine; by PDK3 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q06437 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 5BF049BEE483EF5D
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FASTA

391

43,393

        10         20         30         40         50         60 
MRKMLATVLS QVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYLLEQG PPTSTVLTRE 

        70         80         90        100        110        120 
EALKYYRNMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA CNVGLEAGIN PTDHIITSYR 

       130        140        150        160        170        180 
AHGLCYTRGL SVKSILAELT GRKGGCAKGK GGSMHMYAKN FYGGNGIVGA QVPLGAGVAL 

       190        200        210        220        230        240 
ACKYLKNGQI CLALYGDGAA NQGQVFEAYN MSALWKLPCV FICENNRYGM GTAIERSAAS 

       250        260        270        280        290        300 
TDYHKKGFVI PGLRVNGMDI LSVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI 

       310        320        330        340        350        360 
SYRTREEVQN VRSKSDPIML LRERMISNNL SSVEELKEID ADVKKEVEEA AQFATTDPEP 

       370        380        390 
PLEDLANYLY HQNPPFEVRG AHKWLKFKSV S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNAs encoding the rat testis-specific E1 alpha subunit of the pyruvate dehydrogenase complex: comparison of expression of the corresponding mRNA with that of the somatic E1 alpha subunit." Cullingford T.E., Clark J.B., Phillips I.R. Biochim. Biophys. Acta 1216:149-153(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Pyruvate dehydrogenase E1 alpha isoform in rat testis: cDNA cloning, characterization, and biochemical comparison of the recombinant testis and liver enzymes." Jeng J., Kallarakal A.T., Kim S.F., Popov K.M., Song B.J. Comp. Biochem. Physiol. 120B:205-216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z18878 mRNA. Translation: CAA79318.1. U44125 mRNA. Translation: AAB68458.1. BC078757 mRNA. Translation: AAH78757.1.
IPI	IPI00193263.
PIR	S31416.
RefSeq	NP_446446.1. NM_053994.2.
UniGene	Rn.11126.
3D structure databases
ProteinModelPortal	Q06437.
SMR	Q06437. Positions 31-391.
ModBase	Search...
Proteomic databases
PRIDE	Q06437.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117098.
KEGG	rno:117098.
Organism-specific databases
CTD	5161.
RGD	620095. Pdha2.
Phylogenomic databases
HOVERGEN	HBG001863.
InParanoid	Q06437.
KO	K00161.
OMA	FHYNIAS.
Gene expression databases
Genevestigator	Q06437.
GermOnline	ENSRNOG00000016223. 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...
Other
NextBio	619976.

Entry information

Entry name

ODPAT_RAT

Accession

Primary (citable) accession number: Q06437

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information