Reviewed, UniProtKB/Swiss-Prot P47515 (ODPB_MYCGE)

Names and origin

Protein names

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

Gene names

Name:	pdhB
Ordered Locus Names:	MG273

Organism

Mycoplasma genitalium [Complete proteome] [HAMAP]

Taxonomic identifier

2097 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

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 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.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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_0000162223
Sites
	Binding site	62	1	Thiamine pyrophosphate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47515-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 7C5A0ECCD8A17DD7	FASTA	326	36,026
	10 20 30 40 50 60 MSKIQVNNIE ALNNAMDLAL ERDQNVVLYG QDAGFEGGVF RATKGLQQKY GSERVWDCPI 70 80 90 100 110 120 AENSMAGIGV GAAIGGLKPI VEIQFSGFSF PAMFQIFVHA ARIRNRSRGV YTAPLVVRMP 130 140 150 160 170 180 MGGGIKALEH HSETLEAIYA QIAGLKTVMP SNPYDTKGLF LAAIESPDPV IFFEPKKLYR 190 200 210 220 230 240 AFRQEIPSDY YTVPIGEANL ISEGSELTIV SYGPTMFDLI NLVYSGELKD KGIELIDLRT 250 260 270 280 290 300 ISPWDKQTVF NSVKKTGRLL VVTEAVKSFT TSAEIITSVT EELFTYLKKA PQRVTGFDIV 310 320 VPLARGEKYQ FEINARVIDA VNQLLK

References

[1]

"The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. , Phillips C.A., Merrick J.M., Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C. Science 270:397-403(1995) [PubMed: 7569993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L43967 Genomic DNA. Translation: AAC71495.1.
PIR	B64230.
RefSeq	NP_072940.1.
3D structure databases
HSSP	HSSP built from PDB template 1IK6 based on UniProtKB Q8ZUR7.
ModBase	Search...
Genome annotation databases
GeneID	875399.
GenomeReviews	Gene locus MG273 in contig L43967_GR.
KEGG	mge:MG_273.
TIGR	MG273.
Phylogenomic databases
HOGENOM	P47515.
OMA	P47515. FADPLED.
Enzyme and pathway databases
BioCyc	MGEN243273:MG_273-MON.
BRENDA	1.2.4.1. 110.
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_MYCGE

Accession

Primary (citable) accession number: P47515

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 54 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)