P52904 (ODPB_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial Short name=PDHE1-B EC=1.2.4.1
Organism	Pisum sativum (Garden pea)
Taxonomic identifier	3888 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	359 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 By similarity.
Subcellular location	Mitochondrion matrix.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from electronic annotation. Source: InterPro glycolysis 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 – 19	19	Mitochondrion By similarity
	Chain	20 – 359	340	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000020463
Sites
	Binding site	82	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52904 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5AFE49F165C13C83	FASTA	359	38,793
	10 20 30 40 50 60 MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG EEVGEYQGAY 70 80 90 100 110 120 KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV VEFMTFNFSM QAIDHIINSA 130 140 150 160 170 180 AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ HSHCYASWYG SCPGLKVLVP HSAEDARGLL 190 200 210 220 230 240 KAAIRDPDPV VFLENELLYG ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG 250 260 270 280 290 300 FALKAAEILE KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT 310 320 330 340 350 SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH RSVPLAAAA

References

[1]	Luethy M.H., Miernyk J.A., Randall D.D. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U56697 mRNA. Translation: AAB01223.1.
PIR	T06532.
3D structure databases
ProteinModelPortal	P52904.
SMR	P52904. Positions 25-347.
ModBase	Search...
Protein-protein interaction databases
IntAct	P52904. 1 interaction.
Proteomic databases
PRIDE	P52904.
ProMEX	P52904.
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]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPB_PEA

Accession

Primary (citable) accession number: P52904

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program