Q2YY06 (ODO2_STAAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
EC=2.3.1.61

Alternative name(s):
2-oxoglutarate dehydrogenase complex component E2
Short name=OGDC-E2
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene names

Name:	odhB
Ordered Locus Names:	SAB1268c

Organism

Staphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP]

Taxonomic identifier

273036 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently By similarity.
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
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	Tricarboxylic acid cycle
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	oxoglutarate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	dihydrolipoyllysine-residue succinyltransferase 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 – 422	422	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000288098
Regions
	Domain	2 – 75	74	Lipoyl-binding
Sites
	Active site	393	1	By similarity
	Active site	397	1	By similarity
Amino acid modifications
	Modified residue	42	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2YY06 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: F45D1227F4EC0C95	FASTA	422	46,705
	10 20 30 40 50 60 MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EAGVLSEQLA 70 80 90 100 110 120 SEGDTVEVGQ AIAVIGEGSG NASKENSNDN TPQQNEETNN KKEETTNKSA DNAEVNQTND 130 140 150 160 170 180 YNQQRVNATP SARRYARENG VNLAEVSPKT NDVVRKEDID KKQQAPASTQ TTQQAPAKEE 190 200 210 220 230 240 KKYNQYPTKP VIREKMSRRK KTAAKKLLEV SNNTAMLTTF NEVDMTNVME LRKRKKEQFM 250 260 270 280 290 300 KDHDGTKLGF MSFFTKASVA ALKKYPEVNA EIDGDDMITK QYYDIGVAVS TDDGLLVPFV 310 320 330 340 350 360 RDCDKKNFAE IEAEIANLAV KAREKKLGLD DMVNGSFTIT NGGIFGSMMS TPIINGNQAA 370 380 390 400 410 420 ILGMHSIITR PIAIDQDTIE NRPMMYIALS YDHRIIDGKE AVGFLKTIKE LIENPEDLLL ES

References

[1]	"Molecular correlates of host specialization in Staphylococcus aureus." Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V. PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: bovine RF122 / ET3-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ938182 Genomic DNA. Translation: CAI80957.1.
RefSeq	YP_416745.1. NC_007622.1.
3D structure databases
ProteinModelPortal	Q2YY06.
SMR	Q2YY06. Positions 193-419.
ModBase	Search...
Protein-protein interaction databases
STRING	273036.SAB1268c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI80957; CAI80957; SAB1268c.
GeneID	3793632.
KEGG	sab:SAB1268c.
PATRIC	19523407. VBIStaAur92441_1352.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
KO	K00658.
OMA	GQDIVYK.
ProtClustDB	PRK05704.
Enzyme and pathway databases
BioCyc	SAUR273036:GJVS-1290-MONOMER.
UniPathway	UPA00868; UER00840.
Family and domain databases
Gene3D	3.30.559.10. 1 hit. 4.10.320.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR004167. E3-bd. IPR011053. Single_hybrid_motif. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. PF02817. E3_binding. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_STAAB

Accession

Primary (citable) accession number: Q2YY06

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program