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Reviewed, UniProtKB/Swiss-Prot P26269 (ODPB_ASCSU)

Last modified May 5, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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 lineageEukaryotaMetazoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

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. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

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: 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
P26269-1 [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: 2052042] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-42.

Cross-references

Sequence databases

M38017 mRNA. Translation: AAA29379.1.

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P11177.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.4.1. 649.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
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: May 5, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information