Reviewed, UniProtKB/Swiss-Prot Q9TLS3 (ODPB_CYACA)

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

Cyanidium caldarium

Taxonomic identifier

2771 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Bangiophyceae › Cyanidiales › Cyanidiaceae › Cyanidium

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
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 – 327	327	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000280107
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9TLS3-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0697A6E73817EFF2	FASTA	327	35,946
	10 20 30 40 50 60 MSMMFLYEAL RAAIDEEMGK DSNVFIVGED VGHYGGSYKV TKDLHVKYGD LRVLDAPIAE 70 80 90 100 110 120 NSFTGMAIGA AMTGLRPIVE GMNMGFMLLA FNQISNNLSM LQYTSGGNFN IPVVIRGPGG 130 140 150 160 170 180 IGKQLAAEHS QRLESCFQSI PGLQIVACST AYNAKGLLKS AIIEKKPILF LEHVLLYNLK 190 200 210 220 230 240 GFVPDEEYYL PLDKAEVVRS GSDVTIVTYS RMRYHVLAAV EKLVLNGQDP EIIDLISLKP 250 260 270 280 290 300 LDLHTISKSI KKTHKIVIVE ECAQTGGIAA ELISLINTYL YDELDSPAVR LSSKDVPIPY 310 320 NGNLEKSTLI QPDQIVDVVT NLLQYKT

References

[1]	"The structure and gene repertoire of an ancient red algal plastid genome." Gloeckner G., Rosenthal A., Valentin K.-U. J. Mol. Evol. 51:382-390(2000) [PubMed: 11040290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RK-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF022186 Genomic DNA. Translation: AAF12898.1.
RefSeq	NP_045196.1.
3D structure databases
HSSP	HSSP built from PDB template 1W88 based on UniProtKB P21874.
SMR	Q9TLS3. Positions 3-325.
ModBase	Search...
Genome annotation databases
GeneID	800229.
Enzyme and pathway databases
BRENDA	1.2.4.1. 145.
Family and domain databases
InterPro	IPR009014. Transketo_C/Pyr-ferredox_oxred. 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]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPB_CYACA

Accession

Primary (citable) accession number: Q9TLS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	May 1, 2000
Last modified:	January 19, 2010
This is version 43 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)