P35488 (ODPB_ACHLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

pdhB

Organism

Acholeplasma laidlawii

Taxonomic identifier

2148 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
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).
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
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
	Chain	1 – 327	327	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000162220
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35488 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: F71D6DE807CDBE1C	FASTA	327	35,682
	10 20 30 40 50 60 MAIITLLEAI NQAIDQAMEK DESIVVFGED AGFEGGVFRV TAGLQKKYGE TRVFDTPIAE 70 80 90 100 110 120 SAIVGSAVGM AINGLKPIAE IQFDGFIFPG YTDLVTHAAR MRNRSRGQFT VPMVLRLPHG 130 140 150 160 170 180 GGIRALEHHS EALEVLFGSI PGLKVVTPST PYDAKGLLLA AINDPDPVVF LEPKRIYRAG 190 200 210 220 230 240 KQEVPAEMYE IPIGKAKVVK QGTDMTVVAW GSIVREVEKA VKLVEAEGIS VEIIDLRTIS 250 260 270 280 290 300 PIDEETILNS VKKTGKFMVV TEAVKSYGPA AELITMVNEK AFFHLEAAPV RFTGFDITVP 310 320 LARGEHYHFP QPEKIAAYIR KLAKARP

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M81753 Genomic DNA. Translation: AAA21908.1.
PIR	B42653.
3D structure databases
ProteinModelPortal	P35488.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
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_ACHLA

Accession

Primary (citable) accession number: P35488

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program