Reviewed, UniProtKB/Swiss-Prot P35485 (ODPA_ACHLA)

Names and origin

Protein names

Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha
    EC=1.2.4.1

Gene names

Name:

pdhA

Organism

Acholeplasma laidlawii

Taxonomic identifier

2148 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	345 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

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.
Subunit structure	Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 345	›345	Pyruvate dehydrogenase E1 component subunit alpha		PRO_0000162197
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P35485-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 797F9F67DE0C2995	FASTA	345	38,962
	10 20 30 40 50 60 DQNGKVVNEK MEPKLPKETL LKMYKTAVLG RNADIKALQY QRQGRMLTYA PNMGQEAAQI 70 80 90 100 110 120 GMAAAMEPQD WNSPMYRELN TLLYRGDKLE NVFLYWYGNE RGSIKPEGVK ILPTNIIIGS 130 140 150 160 170 180 QSNIAAGLAM ASKIRKTNEV TAFTIGDGGT AHGEFYEGLN FAASFKAPVV AVIQNNQWAI 190 200 210 220 230 240 STPVRKASNS ETLAQKGVAF GIPYIQVDGN DMLAMYVASK EAMDRARKGD GPTLIEAFTY 250 260 270 280 290 300 RMGPHTTSDD PCSIYRTKEE ENEWAKKDQI ARFKTYLINK GYWSEEEDKK LEEEVLAEIN 310 320 330 340 DTFKKVESYG ANVELIEIFE HTYAEMTPQL KEQYEEHKKY LEGVK

References

[1]	"Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii." Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A. J. Bacteriol. 174:1388-1396(1992) [PubMed: 1735725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M81753 Genomic DNA. Translation: AAA21907.1.
PIR	A42653.
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.4.1. 96506.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017596. Pyrv_DH_E1_asu_subgrp-x. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03181. PDH_E1_alph_x. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_ACHLA

Accession

Primary (citable) accession number: P35485

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)