Reviewed, UniProtKB/Swiss-Prot A2CI50 (ODPB_CHLAT)

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

Chlorokybus atmophyticus (Soil alga)

Taxonomic identifier

3144 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Chlorokybophyceae › Chlorokybales › Chlorokybaceae › Chlorokybus

Protein attributes

Sequence length	335 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 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.
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-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
	Chain	1 – 335	335	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000280103
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2CI50-1 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: E846941B42AF42AF	FASTA	335	36,680
	10 20 30 40 50 60 MAVRFLFEAL QKAIDEEMER EKRVVLIGED IGHYGGSYKV TQGLYGKYGK HRVIDTPIAE 70 80 90 100 110 120 YSFVGAAVGA AATGLIPVVE GMNMAFILLA YSQISNNMGM LCATSGGHFQ VPMVLRGPGG 130 140 150 160 170 180 IGKQLGAEHS QRLESYFQSV PGLQIVTCST PYNAKGLLKS AIRSKNPILF IEHVLLYNLK 190 200 210 220 230 240 GEVPDNDYLL PLEKAELVRE GSDITVLTYS RQRYNVIQAV KVLVEEGYDP EVIDLISLKP 250 260 270 280 290 300 FDMETIGKSI QKTHKVLIVE ECMMTGGISN VLQSLIIDNF FDALDAAPLI LSSPNVPTPY 310 320 330 TGPLEEATVV QTIDIIESIE YGITGKPPKP RTAKK

References

[1]

"A clade uniting the green algae Mesostigma viride and Chlorokybus atmophyticus represents the deepest branch of the Streptophyta in chloroplast genome-based phylogenies." Lemieux C., Otis C., Turmel M. BMC Biol. 5:2-2(2007) [PubMed: 17222354] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAG 48.80.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ422812 Genomic DNA. Translation: ABM87959.1.
RefSeq	YP_001019115.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4783272.
Family and domain databases
InterPro	IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [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]
ProtoNet	Search...

Entry information

Entry name

ODPB_CHLAT

Accession

Primary (citable) accession number: A2CI50

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	February 20, 2007
Last modified:	September 22, 2009
This is version 14 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)