P86219 (ODO2_MESAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
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
E2K

Gene names

Name:

DLST

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length	145 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

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 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB Q01205
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine. UniProtKB Q01205
Cofactor	Binds 1 lipoyl cofactor covalently By similarity. UniProtKB Q01205
Pathway	Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6. UniProtKB Q01205
Subunit structure	Forms a 24-polypeptide structural core with octahedral symmetry By similarity. UniProtKB Q01205
Subcellular location	Mitochondrion By similarity UniProtKB Q01205.
Sequence similarities	Belongs to the 2-oxoacid dehydrogenase family. Contains 1 lipoyl-binding domain.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Lipoyl
Molecular function	Acyltransferase Transferase
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	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 145	›145	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000394748
Regions
	Domain	4 – 31	28	Lipoyl-binding
Sites
	Active site	119	1	Potential UniProtKB Q01205
	Active site	123	1	Potential UniProtKB Q01205
Experimental info
	Non-adjacent residues	21 – 22	2
	Non-adjacent residues	32 – 33	2
	Non-adjacent residues	104 – 105	2
	Non-adjacent residues	132 – 133	2
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P86219 [UniParc]. Last modified June 15, 2010. Version 1. Checksum: 32D674B5DD798BBD	FASTA	145	16,122
	10 20 30 40 50 60 NDVITVQTPA FAESVTEGDV RVEGGTPLFT LRHNLKLGFM SAFVKASAFA LQEQPVVNAV 70 80 90 100 110 120 IDDATKEVVY RDYIDISVAV ATPRGLVVPV IRNVETMNYA DIERVEVRPM MYVALTYDHR 130 140 LIDGREAVTF LRAAVEDPRV LLLDL

References

[1]

"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa." Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S. Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P86219.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00868; UER00840.
Family and domain databases
Gene3D	3.30.559.10. 2 hits.
InterPro	IPR001078. 2-oxoacid_DH_actylTfrase. IPR023213. CAT-like_dom. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 2 hits. [Graphical view]
PROSITE	PS50968. BIOTINYL_LIPOYL. Partial match. PS00189. LIPOYL. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODO2_MESAU

Accession

Primary (citable) accession number: P86219

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	June 15, 2010
Last modified:	March 6, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program