Q8GCY1 (ODO2_BARVB) 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:

sucB

Organism

Bartonella vinsonii subsp. berkhofii

Taxonomic identifier

40933 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella › Bartonella vinsonii

Protein attributes

Sequence length	411 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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently.
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
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 – 411	411	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162258
Regions
	Domain	2 – 76	75	Lipoyl-binding
Sites
	Active site	382	1	By similarity
	Active site	386	1	By similarity
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8GCY1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 4BE837429BDE913A	FASTA	411	43,841
	10 20 30 40 50 60 MTTEIRVPTL GESVTEATVG KWFKKLGEAV AIDEPLVELE TDKVTVEVPS PVAGKLFEII 70 80 90 100 110 120 AKEGDTVEVN ALLGAVEAGA ASVAKSPSSS ETSVSAAPSE LEQSSSSNTM PPAPSAAKLM 130 140 150 160 170 180 AENNIAKSDI LGSGKRGQIL KEDVLNVLAQ GVKTSPPAVS ASSSTPVSVS SSAVAPVQEM 190 200 210 220 230 240 REERVRMTKL RQTIARRLKD AQNTAAMLTT FNEVDMSAVM GLRKRYKDLF EKKHGVKLGF 250 260 270 280 290 300 MGFFTKAVCH ALKELPAVNA EIDGTDIIYK NYVNAGIAVG TDKGLVVPVV RDADQMSLAE 310 320 330 340 350 360 IEKEIGRLGR LARDGKLAVS DMQGGTFTIT NGGVYGSLMS TPILNAPQSG ILGMHAIKER 370 380 390 400 410 AMVVDGQIAI RPMMYLALSY DHRIVDGQEA VTFLVRVKES LEDPERLVLD L

References

[1]

"Molecular characterization of the sucB gene encoding the immunogenic dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp. berkhoffii and Bartonella quintana." Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L. Infect. Immun. 71:4818-4822(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY160679 Genomic DNA. Translation: AAN78227.1.
3D structure databases
ProteinModelPortal	Q8GCY1.
SMR	Q8GCY1. Positions 182-411.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.61. 7855.
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	SSF47005. E3_bd. 1 hit. 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_BARVB

Accession

Primary (citable) accession number: Q8GCY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program