Q06437

PR
Gene name
Pdha2
Protein name
Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
Names
PDHE1-A type II
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:117098
EC number
1.2.4.1: With a disulfide as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-57 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q06437

Entry ID Method Resolution Chain Position Source
AF-Q06437-F1 Predicted AlphaFoldDB

No variants for Q06437

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q06437

No associated diseases with Q06437

1 regional properties for Q06437

Type Name Position InterPro Accession
domain Dehydrogenase, E1 component 68 - 361 IPR001017

Functions

Description
EC Number 1.2.4.1 With a disulfide as acceptor
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
pyruvate dehydrogenase complex Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA; comprises subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3).

1 GO annotations of molecular function

Name Definition
pyruvate dehydrogenase (acetyl-transferring) activity Catalysis of the reaction: pyruvate + lipoamide = S-acetyldihydrolipoamide + CO2.

4 GO annotations of biological process

Name Definition
acetyl-CoA biosynthetic process from pyruvate The chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate.
glucose metabolic process The chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides.
pyruvate metabolic process The chemical reactions and pathways involving pyruvate, 2-oxopropanoate.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P35487 Pdha2 Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial Mus musculus (Mouse) PR
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