Q9R9N5 (ODPA_RHIME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	pdhA
Synonyms:	pdhAalpha
Ordered Locus Names:	R01445
ORF Names:	SMc01030

Organism

Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

266834 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium › Rhizobium meliloti

Protein attributes

Sequence length	348 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
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 – 348	348	Pyruvate dehydrogenase E1 component subunit alpha		PRO_0000162202

Sequences

	Sequence		Length	Mass (Da)
	Q9R9N5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 671DBC015C03CC78	FASTA	348	38,113
	10 20 30 40 50 60 MAPRKSASVS SRKTAAKPAK KDFAGGTIAE FSKEDDLKAY REMLLIRRFE EKAGQLYGMG 70 80 90 100 110 120 FIGGFCHLYI GQEAVVVGMQ LALKEGDQVI TGYRDHGHML ACGMSARGVM AELTGRRGGL 130 140 150 160 170 180 SKGKGGSMHM FSKEKHFYGG HGIVGAQVSL GTGLAFANRY RGNDNVSLAY FGDGAANQGQ 190 200 210 220 230 240 VYESFNMAAL WKLPVIYIVE NNRYAMGTSV SRASAQTDFS QRGASFGIPG YQVDGMDVRA 250 260 270 280 290 300 VKAAADEAVE HCRSGKGPII LEMLTYRYRG HSMSDPAKYR SKDEVQKMRS EHDPIEQVKA 310 320 330 340 RLTDKGWATE DELKQIDKEV RDIVADSADF AQSDPEPDVS ELYTDILL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Symbiotic induction of pyruvate dehydrogenase genes from Sinorhizobium meliloti." Cabanes D., Boistard P., Batut J. Mol. Plant Microbe Interact. 13:483-493(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: RCR2011 / SU47.
[2]	"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F. Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.
[3]	"The composite genome of the legume symbiont Sinorhizobium meliloti." Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J. Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF190792 Genomic DNA. Translation: AAF04587.1. AL591688 Genomic DNA. Translation: CAC46024.1.
RefSeq	NP_385551.1. NC_003047.1.
3D structure databases
ProteinModelPortal	Q9R9N5.
SMR	Q9R9N5. Positions 26-347.
ModBase	Search...
Protein-protein interaction databases
STRING	266834.SMc01030.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC46024; CAC46024; SMc01030.
GeneID	1233098.
KEGG	sme:SMc01030.
PATRIC	23632227. VBISinMel96828_2865.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1071.
HOGENOM	HOG000281336.
KO	K00161.
OMA	FAQNDPE.
ProtClustDB	CLSK806151.
Enzyme and pathway databases
BioCyc	SMEL266834:GJF6-1480-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_RHIME

Accession

Primary (citable) accession number: Q9R9N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program