[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 3-454, AND PROTEIN SEQUENCE OF 69-83. TISSUE=Heart; PubMed=1918017 [NCBI, ExPASy, EBI, Israel, Japan] Nakano K., Matuda S., Yamanaka T., Tsubouchi H., Nakagawa S., Titani K., Ohta S., Miyata T.; "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."; J. Biol. Chem. 266:19013-19017(1991).
[3]	PROTEIN SEQUENCE OF 69-89; 279-287 AND 314-326, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; Lubec G., Chen W.-Q., Afjehi-Sadat L., Diao W.; Submitted (APR-2007) to UniProtKB.

Comments

FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N⁶-(dihydrolipoyl)lysine = CoA + enzyme N⁶-(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: Forms a 24-polypeptide structural core with octahedral symmetry.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
SIMILARITY: Contains 1 lipoyl-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC083858; AAH83858.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D90401; BAA14397.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A41015; A41015.

NP_001006982.2; -.

3D structure databases

HSSP

P07016; 1C4T. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q01205.

Organism-specific databases

RGD

1359615; Dlst.

Gene expression databases

ArrayExpress

Q01205; -.

GermOnline

ENSRNOG00000005061; Rattus norvegicus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0045252;	Cellular component: oxoglutarate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0004149;	Molecular function: dihydrolipoyllysine-residue succinyltransferase activity (inferred from electronic annotation from InterPro).
GO:0031405;	Molecular function: lipoic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003016; 2-oxoA_DHase_lipoyl-BS.
IPR001078; 2Oxoacid_DHase.
IPR000089; Biotin_lipoyl.
IPR006255; SucB.
Graphical view of domain structure.

Pfam

PF00198; 2-oxoacid_dh; 1.
PF00364; Biotin_lipoyl; 1.
Pfam graphical view of domain structure.

ProDom

PD001115; 2Oxoacid_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01347; sucB; 1.

PROSITE

PS50968; BIOTINYL_LIPOYL; 1.
PS00189; LIPOYL; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q01205.

Genome annotation databases

Ensembl

ENSRNOG00000005061; Rattus norvegicus. [Contig view]

GeneID

299201; -.

KEGG

rno:299201; -.

Phylogenomic databases

HOVERGEN

Q01205; -.

Other

NextBio

644993; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Direct protein sequencing; Lipoyl; Mitochondrion; Transferase; Transit peptide; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 68`	`68`	`Mitochondrion.`
`CHAIN`	`69 454`	`386`	`Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial.`	`PRO_0000020475`
`DOMAIN`	`72 144`	`73`	`Lipoyl-binding.`
`ACT_SITE`	`425 425`		`Potential.`
`ACT_SITE`	`429 429`		`Potential.`
`BINDING`	`111 111`		`Lipoyl (covalent) (Potential).`
`CONFLICT`	`13 13`		`S -> M (in Ref. 2; BAA14397).`
`CONFLICT`	`52 54`		`NSS -> TVA (in Ref. 2; BAA14397).`
`CONFLICT`	`164 164`		`Y -> H (in Ref. 2; BAA14397).`
`CONFLICT`	`281 281`		`F -> L (in Ref. 2; BAA14397).`
`CONFLICT`	`448 448`		`R -> A (in Ref. 2; BAA14397).`

Sequence information

Length: 454 AA [This is the length of the unprocessed precursor]

Molecular weight: 48925 Da [This is the MW of the unprocessed precursor]

CRC64: 2818F530F4B7C683 [This is a checksum on the sequence]

        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

Q01205 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools