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Q06437

- ODPAT_RAT

UniProt

Q06437 - ODPAT_RAT

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Protein

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

Gene

Pdha2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

Cofactori

Thiamine pyrophosphate.By similarity

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.By similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: RGD

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: RGD
  2. glucose metabolic process Source: UniProtKB-KW
  3. glycolytic process Source: InterPro
  4. pyruvate metabolic process Source: UniProtKB
  5. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
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 namesi
Name:Pdha2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620095. Pdha2.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: RGD
  2. pyruvate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 391361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrialPRO_0000020449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei294 – 2941Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
Modified residuei301 – 3011Phosphoserine; by PDK3By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ06437.

Expressioni

Tissue specificityi

Testis.1 Publication

Gene expression databases

GenevestigatoriQ06437.

Interactioni

Subunit structurei

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.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ06437.
SMRiQ06437. Positions 31-391.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001863.
InParanoidiQ06437.
KOiK00161.
PhylomeDBiQ06437.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06437-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKMLATVLS QVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYLLEQG
60 70 80 90 100
PPTSTVLTRE EALKYYRNMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA
110 120 130 140 150
CNVGLEAGIN PTDHIITSYR AHGLCYTRGL SVKSILAELT GRKGGCAKGK
160 170 180 190 200
GGSMHMYAKN FYGGNGIVGA QVPLGAGVAL ACKYLKNGQI CLALYGDGAA
210 220 230 240 250
NQGQVFEAYN MSALWKLPCV FICENNRYGM GTAIERSAAS TDYHKKGFVI
260 270 280 290 300
PGLRVNGMDI LSVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI
310 320 330 340 350
SYRTREEVQN VRSKSDPIML LRERMISNNL SSVEELKEID ADVKKEVEEA
360 370 380 390
AQFATTDPEP PLEDLANYLY HQNPPFEVRG AHKWLKFKSV S
Length:391
Mass (Da):43,393
Last modified:June 1, 1994 - v1
Checksum:i5BF049BEE483EF5D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z18878 mRNA. Translation: CAA79318.1.
U44125 mRNA. Translation: AAB68458.1.
BC078757 mRNA. Translation: AAH78757.1.
PIRiS31416.
RefSeqiNP_446446.1. NM_053994.2.
UniGeneiRn.11126.

Genome annotation databases

GeneIDi117098.
KEGGirno:117098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z18878 mRNA. Translation: CAA79318.1 .
U44125 mRNA. Translation: AAB68458.1 .
BC078757 mRNA. Translation: AAH78757.1 .
PIRi S31416.
RefSeqi NP_446446.1. NM_053994.2.
UniGenei Rn.11126.

3D structure databases

ProteinModelPortali Q06437.
SMRi Q06437. Positions 31-391.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q06437.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 117098.
KEGGi rno:117098.

Organism-specific databases

CTDi 5161.
RGDi 620095. Pdha2.

Phylogenomic databases

HOVERGENi HBG001863.
InParanoidi Q06437.
KOi K00161.
PhylomeDBi Q06437.

Miscellaneous databases

NextBioi 619976.
PROi Q06437.

Gene expression databases

Genevestigatori Q06437.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiODPAT_RAT
AccessioniPrimary (citable) accession number: Q06437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

Dasty 3