Reviewed, UniProtKB/Swiss-Prot P26269 (ODPB_ASCSU)

Names and origin

Protein names	Recommended name:     Pyruvate dehydrogenase E1 component subunit beta, mitochondrial       Short name=PDHE1-B     EC=1.2.4.1
Organism	Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Taxonomic identifier	6253 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Nematoda › Chromadorea › Ascaridida › Ascaridoidea › Ascarididae › Ascaris

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. 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 process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion Ref.1
	Chain	28 – 361	334	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000020456
Sites
	Binding site	90	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P26269-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: F04D1C379C28196B	FASTA	361	39,136
	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

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
EMBLGenBankDDBJ	M38017 mRNA. Translation: AAA29379.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P11177.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.4.1. 649.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR015941. Transketolase_C-like. IPR005475. Transketolase_central-reg. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPB_ASCSU

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)