Q68XI8 (ODO2_RICTY) 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:	RT0170

Organism

Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]

Taxonomic identifier

257363 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › Rickettsia typhi

Protein attributes

Sequence length	398 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 – 398	398	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000288097
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	369	1	Potential
	Active site	373	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q68XI8 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 76C55B5C51446A98	FASTA	398	43,823
	10 20 30 40 50 60 MSIKIIIPSL GESVTEATIA KWYKKLGDAV KTDELLLEIE TDKVTLEVNA PCNGTIGKIS 70 80 90 100 110 120 KTDGANVTVG EEVGEINEIA DTDTAWINNK KQEVSQHTSE QLVDKPAMAS NILAPSVQKL 130 140 150 160 170 180 VTENKLDPNN IKGTGRGGRI TKYDVLETIN TTPITIETHA INKTNEERTQ RVRMSRLRKT 190 200 210 220 230 240 IAQRLKDSQN TAAILTTFNE IDMSKVIALR NQYKEEFEKK HTVKLGFMSF FVKATIEALK 250 260 270 280 290 300 LIPSINAEID GDDLLYKNYY DIGVAVGTEQ GLVVPVIRDA DKMSFADIEQ AIGNLAKKAR 310 320 330 340 350 360 EGKLSISDLS GGTFSISNGG VYGSLLSTPI INPPQSGILG LHKTEERAVV IDGKIEIRPM 370 380 390 MYIALSYDHR IIDGKEGVSF LVKIKNLIEN PEKLLLNL

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU03654.1.
RefSeq	YP_067136.1. NC_006142.1.
3D structure databases
HSSP	HSSP built from PDB template 1GHJ based on UniProtKB P20708.
ProteinModelPortal	Q68XI8.
SMR	Q68XI8. Positions 171-395.
ModBase	Search...
Protein-protein interaction databases
STRING	257363.RT0170.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU03654; AAU03654; RT0170.
GeneID	2959241.
KEGG	rty:RT0170.
PATRIC	17909514. VBIRicTyp34752_0176.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
KO	K00658.
OMA	AAMLTTY.
ProtClustDB	PRK05704.
Enzyme and pathway databases
BioCyc	RTYP257363:GJEQ-179-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_RICTY

Accession

Primary (citable) accession number: Q68XI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program