Reviewed, UniProtKB/Swiss-Prot Q01205 (ODO2_RAT)

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):
    Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
      Short name=E2
    E2K

Gene names

Name:

Dlst

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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).
Catalytic activity	Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.
Cofactor	Binds 1 lipoyl cofactor covalently.
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.
Subcellular location	Mitochondrion.
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 Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred from direct assay. Source: RGD NADH metabolic process Inferred from direct assay. Source: RGD tricarboxylic acid cycle Inferred by curator. Source: RGD
Cellular component	microsome Inferred from direct assay. Source: RGD mitochondrion Inferred from direct assay. Source: RGD oxoglutarate dehydrogenase complex Inferred from direct assay. Source: RGD plasma membrane Inferred from direct assay. Source: RGD
Molecular function	chaperone binding Inferred from physical interaction. Source: RGD dihydrolipoyllysine-residue succinyltransferase activity Inferred from direct assay. Source: RGD heat shock protein binding Inferred from physical interaction. Source: RGD 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
	Transit peptide	1 – 68	68	Mitochondrion Ref.2 Ref.3
	Chain	69 – 454	386	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020475
Regions
	Domain	72 – 144	73	Lipoyl-binding
Sites
	Active site	425	1	Potential
	Active site	429	1	Potential
Amino acid modifications
	Modified residue	111	1	N6-lipoyllysine Potential
Experimental info
	Sequence conflict	13	1	S → M in BAA14397. Ref.2
	Sequence conflict	52 – 54	3	NSS → TVA in BAA14397. Ref.2
	Sequence conflict	164	1	Y → H in BAA14397. Ref.2
	Sequence conflict	281	1	F → L in BAA14397. Ref.2
	Sequence conflict	448	1	R → A in BAA14397. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q01205-1 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 2818F530F4B7C683	FASTA	454	48,925
	10 20 30 40 50 60 MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCQGP GYPDSRKMVI NNSSVFSVRF 70 80 90 100 110 120 FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA 130 140 150 160 170 180 NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP ATAYKAAPEA PAAPPPPVAP 190 200 210 220 230 240 VPTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK 250 260 270 280 290 300 EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 310 320 330 340 350 360 AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL 370 380 390 400 410 420 AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHGI FDRPVAVGGK VEVRPMMYVA 430 440 450 LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[2]	"Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site." Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T. J. Biol. Chem. 266:19013-19017(1991) [PubMed: 1918017] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, PROTEIN SEQUENCE OF 69-83. Tissue: Heart.
[3]	Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 69-89; 135-145; 262-308 AND 314-326, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC083858 mRNA. Translation: AAH83858.1. D90401 mRNA. Translation: BAA14397.1.
IPI	IPI00551702.
PIR	A41015.
RefSeq	NP_001006982.2.
UniGene	Rn.99702
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000005061. Rattus norvegicus. [Contig view]
GeneID	299201.
KEGG	rno:299201.
Organism-specific databases
RGD	1359615. Dlst.
Phylogenomic databases
HOVERGEN	Q01205.
Enzyme and pathway databases
BRENDA	2.3.1.61. 248.
Gene expression databases
ArrayExpress	Q01205.
GermOnline	ENSRNOG00000005061. Rattus norvegicus.
Family and domain databases
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 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...
Other Resources
NextBio	644993.

Entry information

Entry name

ODO2_RAT

Accession

Primary (citable) accession number: Q01205
Secondary accession number(s): Q5XI35

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 12, 2005
Last modified:	June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)