Reviewed, UniProtKB/Swiss-Prot P31051 (ODO2_PSEPU)

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

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	58 AA.
Sequence status	Fragment.
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
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from electronic annotation. Source: EC lipoic acid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 58	›58	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex		PRO_0000162265
Sites
	Active site	29	1	By similarity
	Active site	33	1	By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P31051-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 36EC244AA98374E3	FASTA	58	6,691
	10 20 30 40 50 MHNIIQRPMA INGQVVIRPM MYLALSYDHR LIDGKEAVTF LVTIKNLLED PSRLLLDI

References

[1]	"Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida." Palmer J.A., Hatter K., Sokatch J.R. J. Bacteriol. 173:3109-3116(1991) [PubMed: 1902462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G2.
[2]	Sokatch J.R. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M80189 Genomic DNA. Translation: AAA96436.1.
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
SMR	P31051. Positions 1-58.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.61. 403.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. [Graphical view]
ProDom	PD001115. 2Oxoacid_dh. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00189. LIPOYL. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_PSEPU

Accession

Primary (citable) accession number: P31051

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)