Q86HX0 (ODPB_DICDI) 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

Name:	pdhB
ORF Names:	DDB_G0276417

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	356 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.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: dictyBase glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: dictyBase
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 25	25	Mitochondrion Potential
	Chain	26 – 356	331	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000328626
Sites
	Binding site	85	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q86HX0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A259CB6753D1FF3C	FASTA	356	39,068
	10 20 30 40 50 60 MLSSILKKIQ PSLLVNFRII TRTYATKEVT VRDAINSALD EELARDEKVF IMGEEVAQYN 70 80 90 100 110 120 GAYKITKGLF DKYGGDRIID TPITEAGFAG IGVGAAMAGT RPIIEFMTFN FAMQAIDHII 130 140 150 160 170 180 NSSAKTHYMS GGKVFNPIVW RGPNGPPTAV GAQHSQCFAA WYGSVPGLKV VAPWSAADHR 190 200 210 220 230 240 GLLKSAIRDD NPVVYLESEL LYNYKFDLSD QEQDKEYLVP IGKAKVEREG KDVTIVGFSR 250 260 270 280 290 300 IVSNCMEAAE ILAKEGISAE VINLRTIRPI DAETIVNSLK KTNKLVTVEE GWAQSGIGAE 310 320 330 340 350 ISALMMEHAF DYLDAPIERI CGADVPMPYA SNLENAAMVQ TQNIVNAAKR VTQRNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	Bienvenut W.V., Ura S., Insall R.H. Submitted (JUL-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 134-141; 229-240 AND 255-281, MASS SPECTROMETRY. Strain: AX2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000015 Genomic DNA. Translation: EAL69162.1.
RefSeq	XP_643119.1. XM_638027.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P11177.
ProteinModelPortal	Q86HX0.
SMR	Q86HX0. Positions 28-350.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0229442.
Proteomic databases
PRIDE	Q86HX0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0229442; DDB0229442; DDB_G0276417.
GeneID	8620524.
KEGG	ddi:DDB_G0276417.
Organism-specific databases
dictyBase	DDB_G0276417. pdhB.
Phylogenomic databases
eggNOG	COG0022.
KO	K00162.
OMA	QHSQDYS.
ProtClustDB	PTZ00182.
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_DICDI

Accession

Primary (citable) accession number: Q86HX0
Secondary accession number(s): Q551L1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)