Reviewed, UniProtKB/Swiss-Prot Q8MA03 (ODPB_CHAGL)

Names and origin

Protein names

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

Gene names

Name:	pdhB
Synonyms:	odpB

Encoded on

Plastid; Chloroplast

Organism

Chaetosphaeridium globosum

Taxonomic identifier

96477 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Coleochaetophyceae › Coleochaetales › Chaetosphaeridiaceae › Chaetosphaeridium

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Heterodimer of an alpha and a beta chain By similarity.
Subcellular location	Plastid › chloroplast.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Chloroplast Plastid
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
Cellular component	chloroplast 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 – 326	326	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000280101
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8MA03-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 9E99DFC6EBABDB3C	FASTA	326	35,969
	10 20 30 40 50 60 MAEVLLFEAL RDALDEEMQR DPSVLVMGED VGHYGGSYKV TKGFHEKYGD LRLLDTPIAE 70 80 90 100 110 120 NSFTGMAIGA AMTGLRPIVE GMNMGFLLLA FNQIANNAGM LHYTSGGNFK IPIVIRGPGG 130 140 150 160 170 180 VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNGKGLLKS AIRNDNPVIF FEHVLLYNLN 190 200 210 220 230 240 ENLIEQEYLL CLEKAEVVRP GNDITILTYS RMRHHVLQAA KVLVNKGYDP EIIDILSLKP 250 260 270 280 290 300 LDMGTISLSV RKTHKVLIVE ECMRTGGIGA SLRAAILEDL FDYLDAPIQC LSSQDVPTPY 310 320 SGPLEELTVI QPNQIIQAVE EMCKIE

References

[1]

"The chloroplast and mitochondrial genome sequences of the charophyte Chaetosphaeridium globosum: insights into the timing of the events that restructured organelle DNAs within the green algal lineage that led to land plants." Turmel M., Otis C., Lemieux C. Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002) [PubMed: 12161560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: M1311.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF494278 Genomic DNA. Translation: AAM96525.1.
RefSeq	NP_683783.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ModBase	Search...
Genome annotation databases
GeneID	860807.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR005475. Transketo_Cen_R. IPR015941. Transketolase_C-like. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

ODPB_CHAGL

Accession

Primary (citable) accession number: Q8MA03

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	October 1, 2002
Last modified:	November 4, 2008
This is version 32 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)