Reviewed, UniProtKB/Swiss-Prot Q6B8T1 (ODPB_GRATL)

Names and origin

Protein names

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

Gene names

Name:	pdhB
Synonyms:	odpB
Ordered Locus Names:	Grc000123

Encoded on

Plastid; Chloroplast

Organism

Gracilaria tenuistipitata var. liui (Red alga)

Taxonomic identifier

285951 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Florideophyceae › Gracilariales › Gracilariaceae › Gracilaria

Protein attributes

Sequence length	323 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 – 323	323	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000280108
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6B8T1-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: EF7821FA426BFEED	FASTA	323	35,742
	10 20 30 40 50 60 MTEVLMFDAL REATDEEMQN DSSVFILGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE 70 80 90 100 110 120 NSFMGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFQ IPIVIRGPGG 130 140 150 160 170 180 VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVIF FEHVLLYNLK 190 200 210 220 230 240 DELPNDEYFL PLDKAELVRD GLDVTILTYS RMRHHVMQAV VDLVNDGYNP EVIDLISLKP 250 260 270 280 290 300 LDITSIAQSL MKTHKLIIVE ECMKTGGIGA EIIAQINDNY FDFLDAPIVR LSSQDIPTPY 310 320 NGKLEKATVI YPQQIIEAVK SIV

References

[1]

"Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids." Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C. J. Mol. Evol. 59:464-477(2004) [PubMed: 15638458] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY673996 Genomic DNA. Translation: AAT79704.1.
RefSeq	YP_063629.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2943994.
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]
ProtoNet	Search...

Entry information

Entry name

ODPB_GRATL

Accession

Primary (citable) accession number: Q6B8T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	September 13, 2004
Last modified:	November 4, 2008
This is version 28 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)