Reviewed, UniProtKB/Swiss-Prot Q5HPC7 (ODO2_STAEQ)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
      Short name=E2
    EC=2.3.1.61
Alternative name(s):
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene names

Name:	odhB
Synonyms:	sucB
Ordered Locus Names:	SERP0985

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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	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 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 – 420	420	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000288108
Regions
	Domain	2 – 75	74	Lipoyl-binding
Sites
	Active site	391	1	By similarity
	Active site	395	1	By similarity
Amino acid modifications
	Modified residue	42	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5HPC7-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 9A4A04B2923A2F65	FASTA	420	46,080
	10 20 30 40 50 60 MAEVKVPELA ESITEGTIAE WLKNVGDNVD KGEAILELET DKVNVEVVSE EAGVLSEQLA 70 80 90 100 110 120 EEGDTVEVGQ AVAVVGEGQV NTSNDSSNES SQKDEAKEKE TPKQSNPNSS ESENTQDNSQ 130 140 150 160 170 180 QRINATPSAR RHARKNGVDL SEVSGKGNDV LRKDDVENSQ KSSSQTAKSE SKSQNSGSKQ 190 200 210 220 230 240 TNNNPSKPVI REKMSRRKKT AAKKLLEVSN QTAMLTTFNE VDMTNVMDLR KRKKEQFIKD 250 260 270 280 290 300 HDGTKLGFMS FFTKAAVAAL KKYPEVNAEI DGDDMITKQF YDIGIAVSTD DGLLVPFVRD 310 320 330 340 350 360 CDKKNFAEIE QEIANLAVKA RDKKLGLDDM VNGSFTITNG GIFGSMMSTP IINGNQAAIL 370 380 390 400 410 420 GMHSIITRPI AVDKDTIENR PMMYIALSYD HRIIDGKEAV GFLKTIKELI ENPEDLLLES

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000029 Genomic DNA. Translation: AAW54332.1.
RefSeq	YP_188563.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3242078.
GenomeReviews	Gene locus SERP0985 in contig CP000029_GR.
KEGG	ser:SERP0985.
NMPDR	fig|176279.3.peg.1079.
TIGR	SERP0985.
Phylogenomic databases
HOGENOM	Q5HPC7.
OMA	Q5HPC7. LTTYNEV.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP0985-MON.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR004167. E3_bd. IPR006255. SucB. [Graphical view]
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]
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_STAEQ

Accession

Primary (citable) accession number: Q5HPC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	February 15, 2005
Last modified:	June 16, 2009
This is version 35 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)