Reviewed, UniProtKB/Swiss-Prot O13366 (ODPA_KLULA)

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:	PDA1
Ordered Locus Names:	KLLA0F12001g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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 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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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 – ?		Mitochondrion Potential
	Chain	? – 412		Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial		PRO_0000020450
Experimental info
	Sequence conflict	275 – 281	7	YQASKFA → TKL in AAD03773. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O13366-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: CBCC8AB3DC4C7E96	FASTA	412	45,453
	10 20 30 40 50 60 MLSLKAQSSV VGKSSSLRLV RNFSKNVRAL SQVADETKPG DDDLVQIDLP ETSFEGYLLD 70 80 90 100 110 120 VPELSYQTTK SNLLQMYKDM IIVRRMEMAC DALYKAKKIR GFCHSSVGQE AIAVGIENAI 130 140 150 160 170 180 TKRDTVITSY RCHGFTYMRG AAVQAVLAEL MGRRTGVSFG KGGSMHLYAP GFYGGNGIVG 190 200 210 220 230 240 AQVPLGAGLA FAHQYKHEDA CSFALYGDGA SNQGQVFESF NMAKLWNLPA VFCCENNKYG 250 260 270 280 290 300 MGTAAARSSA MTEYFKRGQY IPGLKVNGMD ILAVYQASKF AKDWTVSGNG PIVLEYETYR 310 320 330 340 350 360 YGGHSMSDPG TTYRTRDEIQ HMRSKNDPIA GLKMHLLELG IATEDEIKAY DKAARKYVDE 370 380 390 400 410 QVELADAAPA PEAKMSILFE DVYVPGSETP TLRGRLQEDT WDFAKKSFAF RD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Inactivation of the Kluyveromyces lactis KlPDA1 gene leads to loss of pyruvate dehydrogenase activity, impairs growth on glucose and triggers aerobic alcoholic fermentation." Zeeman A.-M., Luttik M.A.H., Thiele C., van Dijken J.P., Pronk J.T., Steensma H.Y. Microbiology 144:3437-3446(1998) [PubMed: 9884236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC MYA-539 / JBD100.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF023920 Genomic DNA. Translation: AAD03773.1. CR382126 Genomic DNA. Translation: CAG98332.1.
RefSeq	XP_455624.1.
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBase	Search...
Genome annotation databases
GeneID	2894999.
KEGG	kla:KLLA0F12001g.
Phylogenomic databases
HOGENOM	O13366.
OMA	O13366. LEYETYR.
Enzyme and pathway databases
BRENDA	1.2.4.1. 74088.
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_KLULA

Accession

Primary (citable) accession number: O13366
Secondary accession number(s): Q6CKB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 27, 2004
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)