Reviewed, UniProtKB/Swiss-Prot P65635 (ODP2_STAAM)

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
Ordered Locus Names:	SAV1095

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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).
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
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 – 430	430	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex		PRO_0000162288
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	401	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P65635-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 4050074CAE5ACDA4	FASTA	430	46,368
	10 20 30 40 50 60 MAFEFRLPDI GEGIHEGEIV KWFVKAGDTI EEDDVLAEVQ NDKSVVEIPS PVSGTVEEVM 70 80 90 100 110 120 VEEGTVAVVG DVIVKIDAPD AEDMQFKGHD DDSSSKEEPA KEEAPAEQAP VATQTEEVDE 130 140 150 160 170 180 NRTVKAMPSV RKYAREKGVN IKAVSGSGKN GRITKEDVDA YLNGGAPTAS NESAASATSE 190 200 210 220 230 240 EVAETPAAPA AVSLEGDFPE TTEKIPAMRR AIAKAMVNSK HTAPHVTLMD EIDVQALWDH 250 260 270 280 290 300 RKKFKEIAAE QGTKLTFLPY VVKALVSALK KYPALNTSFN EEAGEIVHKH YWNIGIAADT 310 320 330 340 350 360 DRGLLVPVVK HADRKSIFQI SDEINELAVK ARDGKLTADE MKGATCTISN IGSAGGQWFT 370 380 390 400 410 420 PVINHPEVAI LGIGRIAQKP IVKDGEIVAA PVLALSLSFD HRQIDGATGQ NAMNHIKRLL 430 NNPELLLMEG

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000017 Genomic DNA. Translation: BAB57257.1.
RefSeq	NP_371619.1.
3D structure databases
HSSP	HSSP built from PDB template 2PDE based on UniProtKB P11961.
SMR	P65635. Positions 2-79, 121-165.
ModBase	Search...
2-D gel databases
World-2DPAGE	0002:P65635.
Genome annotation databases
GeneID	1121072.
GenomeReviews	Gene locus SAV1095 in contig BA000017_GR.
KEGG	sav:SAV1095.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P65635.
OMA	P65635. YKHYFNI.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV1095-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. [Graphical view]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODP2_STAAM

Accession

Primary (citable) accession number: P65635
Secondary accession number(s): Q99V06

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 33 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)