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P26269 (ODPB_ASCSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Short name=PDHE1-B
EC=1.2.4.1
OrganismAscaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier6253 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

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) By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Tricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Ref.1
Chain28 – 361334Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020456

Sites

Binding site901Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P26269 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: F04D1C379C28196B

FASTA36139,136
        10         20         30         40         50         60 
MAVNGCMRLL RNGLTSACAL EQSVRRLASG TLNVTVRDAL NAALDEEIKR DDRVFLIGEE 

        70         80         90        100        110        120 
VAQYDGAYKI SKGLWKKYGD GRIWDTPITE MAIAGLSVGA AMNGLRPICE FMSMNFSMQG 

       130        140        150        160        170        180 
IDHIINSAAK AHYMSAGRFH VPIVFRGANG AAVGVAQQHS QDFTAWFMHC PGVKVVVPYD 

       190        200        210        220        230        240 
CEDARGLLKA AVRDDNPVIC LENEILYGMK FPVSPEAQSP DFVLPFGQAK IQRPGKDITI 

       250        260        270        280        290        300 
VSLSIGVDVS LHAADELAKS GIDCEVINLR CVRPLDFQTV KDSVIKTKHL VTVESGWPNC 

       310        320        330        340        350        360 
GVGAEISARV TESDAFGYLD GPILRVTGVD VPMPYAQPLE TAALPQPADV VKMVKKCLNV 


Q 

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References

[1]"Characterization of cDNA clones for the beta subunit of pyruvate dehydrogenase from Ascaris suum."
Wheelock M.J., Komuniecki R., Duran E., Johnson K.R.
Mol. Biochem. Parasitol. 45:9-17(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M38017 mRNA. Translation: AAA29379.1.

3D structure databases

ProteinModelPortalP26269.
SMRP26269. Positions 31-360.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP26269.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-18300.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPB_ASCSU
AccessionPrimary (citable) accession number: P26269
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)