Reviewed, UniProtKB/Swiss-Prot Q1RJX4 (ODPA_RICBR)

Names and origin

Protein names

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

Gene names

Name:	pdhA
Ordered Locus Names:	RBE_0259

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

Protein attributes

Sequence length	326 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.

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
Cellular component	intracellular membrane-bounded organelle Inferred from electronic annotation. Source: InterPro
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 alpha		PRO_0000288752

Sequences

	Sequence		Length	Mass (Da)
	Q1RJX4-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 36F16A727359D2E1	FASTA	326	36,853
	10 20 30 40 50 60 MDIKLGKYKP VKEEYIKSFK DMLLLRRFEE KCGQLYGMGE IGGFCHLYIG QEAVISAVDM 70 80 90 100 110 120 VKQKEDSMVT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DVPNKFYGGH 130 140 150 160 170 180 GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMAALW GLPVVYIIEN 190 200 210 220 230 240 NEYSMGTSVA RSTFMRDLYK KGESFGIKGF QLNGMDFEEM YDGVKQAAEY VRENSMPLIL 250 260 270 280 290 300 EVKTYRYRGH SMSDPAKYRS KEEVETYKER DPITEIRKII LENNYASEAD LKEIEQSVKE 310 320 IVKEAVEFSE NSPLPNEEEL YTQIYV

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000087 Genomic DNA. Translation: ABE04340.1.
RefSeq	YP_537429.1.
3D structure databases
SMR	Q1RJX4. Positions 11-325.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RJX4.
Genome annotation databases
GeneID	3995883.
GenomeReviews	Gene locus RBE_0259 in contig CP000087_GR.
KEGG	rbe:RBE_0259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1071.
HOGENOM	HBG753263.
OMA	IVENNRY.
Enzyme and pathway databases
BioCyc	RBEL336407:RBE_0259-MONOMER.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPA_RICBR

Accession

Primary (citable) accession number: Q1RJX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 16, 2006
Last modified:	February 9, 2010
This is version 30 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)