Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

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P86222 (ODPB_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 12. 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 beta, mitochondrial
Short name=PDHE1-B
EC=1.2.4.1

Gene names

Name:

PDHB

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length	211 AA.
Sequence status	Fragments.
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 By similarity. UniProtKB P11177
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂. UniProtKB P11177
Cofactor	Thiamine pyrophosphate By similarity. UniProtKB P11177
Subunit structure	Heterotetramer of two PDHA1 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 UniProtKB P11177.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: UniProtKB glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC pyruvate dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – ›211

›211

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

PRO_0000394306

Amino acid modifications

Modified residue

Phosphotyrosine By similarity UniProtKB Q9D051

Experimental info

Non-adjacent residues

35 – 36

Non-adjacent residues

133 – 134

Non-terminal residue

211

Sequences

Sequence

Length

Mass (Da)

Tools

P86222 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 0F24DCE9BB09B3E7
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FASTA

211

23,010

        10         20         30         40         50         60 
EAINQGMDEE LERDEKVFLL GEEVAQYDGA YKVSRTYYMS AGLQPVPIVF RGPNGASAGV 

        70         80         90        100        110        120 
AAQHSQCFAA WYGHCPGLKV VSPWNSEDAK GLIKSAIRDD NPVVMLENEL MYGVAFELPT 

       130        140        150        160        170        180 
EAQSKDFLIP IGKEGIECEV INLRTIRPMD IEAIEASVMK TNHLVTVEGG WPQFGVGAEI 

       190        200        210 
CARIMEGPAF NFLDAPAVRV TGADVPMPYA K

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References

[1]

"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P86222.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR027110. PDHB. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
PANTHER	PTHR11624:SF11. PTHR11624:SF11. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPB_MESAU

Accession

Primary (citable) accession number: P86222

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	May 18, 2010
Last modified:	April 3, 2013
This is version 12 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

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