Reviewed, UniProtKB/Swiss-Prot P51266 (ODPB_PORPU)

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

Porphyra purpurea

Taxonomic identifier

2787 [NCBI]

Taxonomic lineage

Eukaryota › Rhodophyta › Bangiophyceae › Bangiales › Bangiaceae › Porphyra

Protein attributes

Sequence length	331 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.
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 – 331	331	Pyruvate dehydrogenase E1 component subunit beta		PRO_0000162219
Sites
	Binding site	60	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51266-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 12D1B9467D4DC993	FASTA	331	36,394
	10 20 30 40 50 60 MSKVFMFDAL RAATDEEMEK DLTVCVIGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE 70 80 90 100 110 120 NSFTGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFT LPLVIRGPGG 130 140 150 160 170 180 VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVVF FEHVLLYNLQ 190 200 210 220 230 240 EEIPEDEYLI PLDKAEVVRK GKDITILTYS RMRHHVTEAL PLLLNDGYDP EVLDLISLKP 250 260 270 280 290 300 LDIDSISVSV KKTHRVLIVE ECMKTAGIGA ELIAQINEHL FDELDAPVVR LSSQDIPTPY 310 320 330 NGSLEQATVI QPHQIIDAVK NIVNSSKTIT T

References

[1]	"Complete nucleotide sequence of the Porphyra purpurea chloroplast genome." Reith M.E., Munholland J. Plant Mol. Biol. Rep. 13:333-335(1995) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Avonport.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U38804 Genomic DNA. Translation: AAC08152.1.
PIR	S73187.
RefSeq	NP_053876.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ModBase	Search...
Genome annotation databases
GeneID	809895.
Enzyme and pathway databases
BRENDA	1.2.4.1. 279956.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR015941. Transketolase_C-like. IPR005475. Transketolase_central-reg. [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_PORPU

Accession

Primary (citable) accession number: P51266

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 49 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)