Reviewed, UniProtKB/Swiss-Prot O44451 (ODPB_CAEEL)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
    EC=1.2.4.1

Gene names

ORF Names:

C04C3.3

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	352 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 CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
Subcellular location	Mitochondrion matrixBy similarity.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	embryonic development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of growth rate Inferred from mutant phenotype. Source: WormBase
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O45924	1	EBI-326559,EBI-330432
mdf-2	Q9NGT3	1	EBI-326559,EBI-328699
sdz-38	Q09620	1	EBI-326559,EBI-332504

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 21	21	Mitochondrion Potential
	Chain	22 – 352	331	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000042638
Sites
	Binding site	81	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O44451-1 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: 37F4A4A28C8ADECA	FASTA	352	38,141
	10 20 30 40 50 60 MALRKCGNLF VARLAGTSTR AASTMTVRDA LNQAMDEEIK RDDRVFLMGE EVAQYDGAYK 70 80 90 100 110 120 ISKGLWKKHG DKRVVDTPIT EMGFAGIAVG AAFAGLRPIC EFMTFNFSMQ AIDQIINSAA 130 140 150 160 170 180 KTYYMSAGRV PVPIVFRGPN GAAAGVAAQH SQDFSAWYAH CPGLKVVCPY SAEDAKGLLK 190 200 210 220 230 240 AAIRDDNPVV FLENEILYGQ SFPVGDEVLS DDFVVPIGKA KIERAGDHVT IVSYSRGVEF 250 260 270 280 290 300 SLEAAKQLEA IGVSAEVINL RSLRPFDFES IRQSVHKTHH LVSVETGWPF AGIGSEIAAQ 310 320 330 340 350 VMESDVFDQL DAPLLRVTGV DVPMPYTQTL EAAALPTAEH VVKAVKKSLN IA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	Bienvenut W.V. Submitted (SEP-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 130-137; 237-246 AND 262-272, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF038606 Genomic DNA. Translation: AAB92024.2.
PIR	T32598.
RefSeq	NP_500340.1.
UniGene	Cel.7275
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P11177.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:24348N.
IntAct	O44451.
Genome annotation databases
Ensembl	C04C3.3. Caenorhabditis elegans. [Contig view]
GeneID	177108.
KEGG	cel:C04C3.3.
Organism-specific databases
WormBase	WBGene00015413. C04C3.3.
WormPep	C04C3.3. CE27647. [WorfDB]
Gene expression databases
ArrayExpress	O44451.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR005475. Transketo_Cen_R. IPR015941. Transketolase_C-like. [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...
Other Resources
NextBio	895372.

Entry information

Entry name

ODPB_CAEEL

Accession

Primary (citable) accession number: O44451

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 1, 2001
Last modified:	November 25, 2008
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project