Reviewed, UniProtKB/Swiss-Prot Q92J43 (ODO2_RICCN)

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:	sucB
Ordered Locus Names:	RC0226

Organism

Rickettsia conorii [Complete proteome] [HAMAP]

Taxonomic identifier

781 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	395 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 – 395	395	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162268
Regions
	Domain	1 – 76	76	Lipoyl-binding
Sites
	Active site	366	1	Potential
	Active site	370	1	Potential
Amino acid modifications
	Modified residue	43	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	Q92J43-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 6DAB5E9A086F5A35	FASTA	395	42,798
	10 20 30 40 50 60 MRVKIIVPSL GESITEATIA KWYKKQGDSV KTDELLLEIE TEKVTLEVNA PCNGTIGKIS 70 80 90 100 110 120 KTEGANVAVG EEIGEINEGA SANTAGTNNE SAKAQAVTQP TSEKPAVANN TLAPSVQKLV 130 140 150 160 170 180 TENKLDPNNI KGTGRDGRIT KGDVLATINT TTTSAPAISK SNEERVQRVR MSRLRKTIAQ 190 200 210 220 230 240 RLKDSQNTAA ILTTFNEIDM SKVIALRNQY KEEFEKKHAV KLGFMSFFVK ATIEALKLIP 250 260 270 280 290 300 SVNAEIDGDD LVYKNYYDIG VAVGTEQGLV VPVVRDADKM GFAEVEKTIG ILAKQAREGK 310 320 330 340 350 360 LSMADLSGGT FSISNGGVYG SLLSTPIINP PQSGILGLHK TEERAVVIDG KIEIRPMMYI 370 380 390 ALSYDHRIID GKEGVSFLVK IKQLIENPEK LLLNL

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006914 Genomic DNA. Translation: AAL02764.1.
PIR	B97728.
RefSeq	NP_359863.1.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	927964.
GenomeReviews	Gene locus RC0226 in contig AE006914_GR.
KEGG	rco:RC0226.
NMPDR	fig|272944.1.peg.226.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q92J43.
OMA	Q92J43. LTTYNEV.
Enzyme and pathway databases
BioCyc	RCON272944:RC0226-MON.
BRENDA	2.3.1.61. 267518.
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]
Gene3D	G3DSA:4.10.320.10. E3_bd. 1 hit.
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_RICCN

Accession

Primary (citable) accession number: Q92J43

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 53 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)