Reviewed, UniProtKB/Swiss-Prot Q9R9N3 (ODP2_RHIME)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
    EC=2.3.1.12
Alternative name(s):
    E2
    Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex

Gene names

Name:	pdhC
Synonyms:	pdhB
Ordered Locus Names:	R01447
ORF Names:	SMc01032

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	447 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	Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW pyruvate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	pyruvate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular function	dihydrolipoyllysine-residue acetyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162284
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	420	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R9N3-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 48B1CAC4E2FDC2AC	FASTA	447	46,140
	10 20 30 40 50 60 MPINITMPAL SPTMEEGNLA KWLVKEGDKV KSGDVIAEIE TDKATMEVEA VDEGTVAKIV 70 80 90 100 110 120 VPAGTEGVKV NALIAVLAAE GEDVATAAKG GNGAAGAVPA PKPKETAETA PAAAPAPAAA 130 140 150 160 170 180 PAPQAAAPAS PAPADGEGKR IFSSPLARRL AKEAGIDLSA IAGSGPHGRV VKKDVETAVS 190 200 210 220 230 240 GGAAKPAGAP AAAPAPATLA KGMSEDAVLK LFEPGSYELV PHDGMRKTIA KRLVESKQTI 250 260 270 280 290 300 PHFYVSVDCE LDALMALRAQ LNAAAPEKDG KPVYKLSVND MVIKALALAL RDVPDANVSW 310 320 330 340 350 360 TDQNMVKHKH ADVGVAVSIP GGLITPIVRQ AELKSLSAIS NEMKDLGKRA KERKLKPEEY 370 380 390 400 410 420 QGGTTAVSNM GMMGVKDFAA VVNPPHATIL AVGAGEDRVV VRNKEMVIAN VMTVTLSTDH 430 440 RCVDGALGAE LLAAFKRYIE NPMGMLV

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: 10796014] [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: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF190792 Genomic DNA. Translation: AAF04589.1. AL591688 Genomic DNA. Translation: CAC46026.1.
RefSeq	NP_385553.1.
3D structure databases
SMR	Q9R9N3. Positions 3-87, 139-186, 215-447.
ModBase	Search...
Genome annotation databases
GeneID	1233100.
GenomeReviews	Gene locus R01447 in contig AL591688_GR.
KEGG	sme:SMc01032.
NMPDR	fig|266834.1.peg.2741.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG630916.
OMA	ANEERTY.
Enzyme and pathway databases
BioCyc	SMEL266834:SMC01032-MONOMER.
BRENDA	2.3.1.12. 142.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR006257. AcTrfase_Pyrv_DH_cplx_L. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. IPR011053. Single_hybrid_motif. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
TIGRFAMs	TIGR01349. PDHac_trf_mito. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_RHIME

Accession

Primary (citable) accession number: Q9R9N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 71 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)