Reviewed, UniProtKB/Swiss-Prot P52993 (ODO2_RALEH)

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
Synonyms:	odhB
Ordered Locus Names:	H16_A2324

Organism

Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP]

Taxonomic identifier

381666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	416 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).
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.
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 – 416	416	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162253
Regions
	Domain	1 – 77	77	Lipoyl-binding
Sites
	Active site	387	1	By similarity
	Active site	391	1	By similarity
Amino acid modifications
	Modified residue	44	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	P52993-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 100D839352D0A8DF	FASTA	416	43,250
	10 20 30 40 50 60 MAIVDVKVPQ LSESVAEATM LNWKKKPGEA VAQDEILIEI ETDKVVLEVP APSAGVLSII 70 80 90 100 110 120 VKNDGDTVVA DEIIAKIDTE ATAGAAAPAA AAPAPAAAAP APAAAVAAPA AAGGVAMPSA 130 140 150 160 170 180 AKLMAEAGLS AGQVAGTGKD GRITKGDALA AAAAPAAKAA PAPAAAKPAL QQVSAPVDFA 190 200 210 220 230 240 ALGDRPEERV PMSRLRARIA ERLLQSQSTN AILTTFNEVN MKPVMDLRNK YKDRFEKEHG 250 260 270 280 290 300 VKLGFMSFFV KAAVHALKKF PLINASIDGN DIVYHGYFDI GIAVGSPRGL VVPILRNADQ 310 320 330 340 350 360 MSLADIEKKI AEFGVKARDG KLSLEELTGG TFSISNGGVF GSMLSTPIIN PPQSAILGVH 370 380 390 400 410 ATKDRPVVED GQIVIRPMNY LAMSYDHRII DGREAVLGLV AMKDALEDPA RLLLDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate dehydrogenase complex." Hein S., Steinbuechel A. FEMS Microbiol. Lett. 136:231-238(1996) [PubMed: 8867378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X91877 Genomic DNA. Translation: CAA62981.1. AM260479 Genomic DNA. Translation: CAJ93420.1.
PIR	T44423.
RefSeq	YP_726788.1.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	4249724.
GenomeReviews	Gene locus H16_A2324 in contig AM260479_GR.
KEGG	reh:H16_A2324.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P52993.
OMA	P52993. LTTYNEV.
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_RALEH

Accession

Primary (citable) accession number: P52993
Secondary accession number(s): Q0K9A1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 71 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)