P49432

PR
Gene name
Pdhb
Protein name
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Names
PDHE1-B
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:289950
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)

1-61 (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 P49432

Entry ID Method Resolution Chain Position Source
AF-P49432-F1 Predicted AlphaFoldDB

No variants for P49432

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49432

No associated diseases with P49432

2 regional properties for P49432

Type Name Position InterPro Accession
domain Transketolase-like, pyrimidine-binding domain 33 - 208 IPR005475
domain Transketolase, C-terminal domain 226 - 349 IPR033248

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 pyruvate dehydrogenase complex Complex that carries out the oxidative decarboxylation of pyruvate to form acetyl-CoA in eukaryotes; includes subunits possessing three catalytic activities: pyruvate dehydrogenase (E1), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The This Eukaryotic form usually contains more subunits than its bacterial counterpart; for example, one known complex contains 30 E1 dimers, 60 E2 monomers, and 6 E3 dimers as well as a few copies of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase.
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.

3 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.
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.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11966 PDHB Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Bos taurus (Bovine) PR
P11177 PDHB Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Homo sapiens (Human) PR
Q9D051 Pdhb Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV
70 80 90 100 110 120
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
130 140 150 160 170 180
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS
190 200 210 220 230 240
EDAKGLIKSA IRDDNPVVML ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV
250 260 270 280 290 300
AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG
310 320 330 340 350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI