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0ODPB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePDHB
DescriptionPyruvate dehydrogenase e1 component beta subunit, mitochondrial precursor (ec 1.2.4.1) (pdhe1-b).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004739 pyruvate dehydrogenase (acetyl-transferring... (TAS)
0006099 tricarboxylic acid cycle (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Transketolase () (TK) catalyzes the reversible transfer of atwo-carbon ketol unit from xylulose 5-phosphate to an aldose receptor.uch asribose 5-phosphate.o form sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate. This enzyme.ogether with transaldolase.rovides a link betweenthe glycolytic and pentose-phosphate pathways.TK requires thiamine pyrophosphate as a cofactor. In most sources where TK hasbeen purified.t is a homodimer of approximately 70 Kd subunits. TK sequencesfrom a variety of eukaryotic and prokaryotic sources .how that theenzyme has been evolutionarily conserved.In the peroxisomes of methylotrophic yeast Hansenula polymorpha.here is ahighly related enzyme.ihydroxy-acetone synthase (DHAS) () (alsoknown as formaldehyde transketolase).hich exhibits a very unusualspecificity by including formaldehyde amongst its substrates. 1-deoxyxylulose-5-phosphate synthase (DXP synthase) is an enzyme so farfound in bacteria (gene dxs) and plants (gene CLA1) which catalyzes thethiamine pyrophosphoate-dependent acyloin condensation reaction between carbonatoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (dxp). precursor in the biosynthetic pathway toisoprenoids.hiamine (vitamin B1).nd pyridoxol (vitamin B6). DXP synthaseis evolutionary related to TK. The N-terminal section.ontains a histidine residue which appears to function inproton transfer during catalysis . In the centralsection there are conserved acidic residues that are part of the active cleftand may participate in substrate-binding .This family includes transketolase enzymes and also partially matches to 2-oxoisovalerate dehydrogenasebeta subunit . Both these enzymesutilise thiamine pyrophosphate as a cofactor.uggestingthere may be common aspects in their mechanism of catalysis.
  IPR005475:Transketolase, central region
Transketolase () (TK) catalyzes the reversible transfer of atwo-carbon ketol unit from xylulose 5-phosphate to an aldose receptor.uch asribose 5-phosphate.o form sedoheptulose 7-phosphate and glyceraldehyde 3-phosphate. This enzyme.ogether with transaldolase.rovides a link betweenthe glycolytic and pentose-phosphate pathways.TK requires thiamine pyrophosphate as a cofactor. In most sources where TK hasbeen purified.t is a homodimer of approximately 70 Kd subunits. TK sequencesfrom a variety of eukaryotic and prokaryotic sources .how that theenzyme has been evolutionarily conserved.In the peroxisomes of methylotrophic yeast Hansenula polymorpha.here is ahighly related enzyme.ihydroxy-acetone synthase (DHAS) () (alsoknown as formaldehyde transketolase).hich exhibits a very unusualspecificity by including formaldehyde amongst its substrates. 1-deoxyxylulose-5-phosphate synthase (DXP synthase) is an enzyme so farfound in bacteria (gene dxs) and plants (gene CLA1) which catalyzes thethiamine pyrophosphoate-dependent acyloin condensation reaction between carbonatoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (dxp). precursor in the biosynthetic pathway toisoprenoids.hiamine (vitamin B1).nd pyridoxol (vitamin B6). DXP synthaseis evolutionary related to TK.The N-terminal section.ontains a histidine residue which appears to function inproton transfer during catalysis . In the centralsection there are conserved acidic residues that are part of the active cleftand may participate in substrate-binding .This family includes transketolase enzymes and also partially matches to 2-oxoisovalerate dehydrogenasebeta subunit . Both these enzymesutilise thiamine pyrophosphate as a cofactor.uggestingthere may be common aspects in their mechanism of catalysis.
  IPR005476:Transketolase, C-terminal
Transketolase C-terminal-like domains can be found in a number of different enzymes.ncluding the C-terminal domain of the pyruvate dehydrogenase E1 component .he C-terminal domain of branched-chain alpha-keto acid dehydrogenases .nd domain II of pyruvate-ferredoxin oxidoreductase (PFOR) . Structural studies reveal this domain to comprise of three layers alpha/beta/alpha. The mixed beta sheet consists of five strands in the order 13245.here strand 1 is antiparallel to the others.
  IPR009014:Transketolase, C-terminal-like
IPR005475:Transket_pyr 
Evalue:-65.2757263183594 
Location:31-208IPR005476:Transketolase_C 
Evalue:-55.5376014709473 
Location:226-349
SequencesProtein: ODPB_HUMAN (359 aa)
mRNA: NM_000925
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK00162
  Level 3 annotation:
    pyruvate dehydrogenase E1 component, beta subunit
  Level 2 annotation:
    Glycolysis / Gluconeogenesis
    Pyruvate metabolism
    Butanoate metabolism
    Valine
     leucine and isoleucine biosynthesis
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 184 residues, 58388397-58388946Exon2: 49 residues, 58389239-58389381Exon3: 32 residues, 58390474-58390566Exon4: 39 residues, 58390894-58391005Exon5: 97 residues, 58391423-58391709Exon6: 14 residues, 58392359-58392395Exon7: 23 residues, 58392497-58392560Exon8: 38 residues, 58392643-58392751Exon9: 20 residues, 58394397-58394451Exon10: 22 residues, 58394534-58394594Exon11: 2 residues, -Jump to ODPB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4613 58388397-58394594 ~-6K 25949(PDHB)(-)Loci: 3362 57969188-58133015 ~-164K 25933(FLNB)(+)Link out to UCSC