Q1RHI5 (ODO2_RICBR) 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
Ordered Locus Names:	RBE_1098

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › belli group › Rickettsia bellii

Protein attributes

Sequence length	400 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 – 400	400	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000288095
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	371	1	Potential
	Active site	375	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q1RHI5 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 2C8334C1FA6F9A10	FASTA	400	43,078
	10 20 30 40 50 60 MGVKIIVPSL GESVTEATIA KWYKKEGDAV KTDELLLEIE TEKVTLEVNS PCNGTIGKII 70 80 90 100 110 120 KADGANVAVG EEIGDINEGE AVATNSNEAA KPQTASQPVP EKVPKKPAVA NNTLAPSVQK 130 140 150 160 170 180 LVTENKLDPN NIKGTGKDGR ITKGDVLETM NAPTPAATST TSSAKASEER VERVRMSRLR 190 200 210 220 230 240 KTIAQRLKDS QNTAAILTTF NEIDMSKVIA LRGKYKDEFE KKHGVKLGFM SFFVRATIEA 250 260 270 280 290 300 LKLIPSVNAE IDGDDLVYKN YYDIGVAVGT EQGLVVPVVR DADKMGFADI EKTIGGLAKK 310 320 330 340 350 360 ARDGKLSMAD LSGGTFSISN GGVYGSLLST PIINPPQSGI LGLHKTEERV VAIDGKIEIR 370 380 390 400 PMMYIALSYD HRIIDGKEAV SFLVKIKELI ESPEKLLLNL

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RML369-C.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000087 Genomic DNA. Translation: ABE05179.1.
RefSeq	YP_538268.1. NC_007940.1.
3D structure databases
ProteinModelPortal	Q1RHI5.
SMR	Q1RHI5. Positions 172-400.
ModBase	Search...
Protein-protein interaction databases
STRING	336407.RBE_1098.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE05179; ABE05179; RBE_1098.
GeneID	3995009.
KEGG	rbe:RBE_1098.
PATRIC	17883773. VBIRicBel102610_1239.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
KO	K00658.
OMA	AAMLTTY.
ProtClustDB	PRK05704.
Enzyme and pathway databases
BioCyc	RBEL336407:GJCY-1131-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	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_RICBR

Accession

Primary (citable) accession number: Q1RHI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program