O44451 (ODPB_CAEEL) 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

Gene names

ORF Names:

C04C3.3

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › 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 CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB P11177
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. UniProtKB P11177
Cofactor	Thiamine pyrophosphate By similarity. UniProtKB P11177
Subunit structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
Subcellular location	Mitochondrion matrix By similarity UniProtKB P11177.

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 Reference proteome
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 mitochondrion Inferred from direct assay PubMed 20188671. Source: WormBase
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 – 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 UniProtKB P11177

Sequences

	Sequence		Length	Mass (Da)
	O44451 [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] [Europe PMC] [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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FO080230 Genomic DNA. Translation: CCD62196.1.
PIR	T32598.
RefSeq	NP_500340.1. NM_067939.5.
3D structure databases
ProteinModelPortal	O44451.
SMR	O44451. Positions 25-351.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-24348N.
IntAct	O44451. 5 interactions.
MINT	MINT-1052850.
STRING	6239.C04C3.3.2.
Proteomic databases
PaxDb	O44451.
PRIDE	O44451.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C04C3.3.1; C04C3.3.1; C04C3.3. C04C3.3.2; C04C3.3.2; C04C3.3.
GeneID	177108.
KEGG	cel:CELE_C04C3.3.
UCSC	C04C3.3.1. c. elegans.
Organism-specific databases
CTD	177108.
WormBase	C04C3.3; CE27647; WBGene00015413.
Phylogenomic databases
eggNOG	COG0022.
GeneTree	ENSGT00530000063423.
HOGENOM	HOG000281450.
InParanoid	O44451.
KO	K00162.
OMA	QHSQDYS.
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...
Other
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:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project