Q54C70 (ODPA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Short name=PDHE1-A
EC=1.2.4.1

Gene names

Name:	pdhA
ORF Names:	DDB_G0292994

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	377 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.
Enzyme regulation	E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity.
Subunit structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
Subcellular location	Mitochondrion matrix By similarity.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome 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 matrix Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from direct assay Ref.2. Source: dictyBase 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 – 26	26	Mitochondrion Potential
	Chain	27 – 377	351	Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial		PRO_0000327983

Sequences

	Sequence		Length	Mass (Da)
	Q54C70 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: BD3481894B7348C3	FASTA	377	41,988
	10 20 30 40 50 60 MLSNFLKVNS KALGHIRTFA SKSGEIKHNF KKADTYLCDG PSDSTVTNKD ELISFFTEMS 70 80 90 100 110 120 RFRRLETVCD GLYKKKLIRG FCHLYTGQEA VCAGLESAIT KDDHIITAYR DHTYMLSRGA 130 140 150 160 170 180 TPEEIFAELL MKETGCSKGK GGSMHMFTKN FYGGNGIVGA QCPLGAGIAF AQKYNKTGNV 190 200 210 220 230 240 CLAMYGDGAA NQGQLFEAFN MASLWKLPVI FICENNKYGM GTSQKRSTAG HDFYTRGHYV 250 260 270 280 290 300 AGLKVDGMDV FAVKEAGKYA AEWCRAGNGP IILEMDTYRY VGHSMSDPGI TYRTREEVNH 310 320 330 340 350 360 VRQTRDPIEN IRQIILDNKI ATEDQLAAIE ETVRDEMEKA SEKAIAAPLP QARELFTNVY 370 LQEVPVRGVE FVNSFKP

References

[1]

"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.

[2]

"Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake." Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M., Soldati T. Mol. Cell. Proteomics 5:2228-2243(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: AX2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000199 Genomic DNA. Translation: EAL60849.1.
RefSeq	XP_629349.1. XM_629347.1.
3D structure databases
ProteinModelPortal	Q54C70.
SMR	Q54C70. Positions 25-366.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDB_0230193.
Proteomic databases
PRIDE	Q54C70.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0230193; DDB0230193; DDB_G0292994.
GeneID	8629073.
KEGG	ddi:DDB_G0292994.
Organism-specific databases
dictyBase	DDB_G0292994. pdhA.
Phylogenomic databases
eggNOG	COG1071.
KO	K00161.
OMA	FAQNDPE.
ProtClustDB	CLSZ2429333.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_DICDI

Accession

Primary (citable) accession number: Q54C70

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	May 29, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)