Reviewed, UniProtKB/Swiss-Prot Q9N0F1 (ODO2_PIG)

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
    E2o
    PE2o

Gene names

Name:

DLST

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	455 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). Ref.1
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 By similarity.
Subcellular location	Mitochondrion. Ref.1
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	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 68	68	Mitochondrion
	Chain	69 – 455	387	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020474
Regions
	Domain	72 – 144	73	Lipoyl-binding
	Region	221 – 453	233	Catalytic
	Compositional bias	151 – 215	65	Pro-rich
Sites
	Active site	426	1	Potential
	Active site	430	1	Potential
Amino acid modifications
	Modified residue	111	1	N6-lipoyllysine Potential
Experimental info
	Mutagenesis	374	1	S → A: Loss of activity.
	Mutagenesis	426	1	H → C: 16% of activity.
	Mutagenesis	430	1	D → A, E or N: Loss of activity.
	Mutagenesis	451 – 453	3	LLL → AAA or DDD: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	Q9N0F1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 563B5E7455C842FA	FASTA	455	48,977
	10 20 30 40 50 60 MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGISLCQGP GYPDSRKIVI SNSSVLNVRF 70 80 90 100 110 120 FRTTAVCKDD VITVKTPAFA ESVTEGDVRW EKAVGDTVAE DEVVCEIETD KTSVQVPSPA 130 140 150 160 170 180 NGVIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAEAP AAAAPKAEPA VSAVPPPPAA 190 200 210 220 230 240 SIPTQMPPVP SPPQPLTSKP VSAVKPTAAP PVAEPGAVKG LRAEHREKMN RMRQRIAQRL 250 260 270 280 290 300 KEAQNTCAML TTFNEIDMSN IQDMRARHKE AFLKKHNLKL GFMSAFVKAS AFALQEQPVV 310 320 330 340 350 360 NAVIDDTTKE VVYRDYIDIS VAVATPRGLV VPVIRNVETM NYADIERTIS ELGEKARKNE 370 380 390 400 410 420 LAIEDMDGGT FTISNGGVFG SLFGTPIINP PQSAILGMHA IVDRPVAVGG KVEIRPMMYV 430 440 450 ALTYDHRLID GREAVTFLRK IKAAVEDPRV LLLDL

References

[1]

"Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex." Koike K., Suematsu T., Ehara M. Eur. J. Biochem. 267:3005-3016(2000) [PubMed: 10806400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS. Tissue: Brain cortex and Heart.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB035206 mRNA. Translation: BAA95700.1.
RefSeq	NP_999562.1.
UniGene	Ssc.2730
3D structure databases
HSSP	HSSP built from PDB template 1C4T based on UniProtKB P07016.
ModBase	Search...
Genome annotation databases
GeneID	397690.
KEGG	ssc:397690.
Phylogenomic databases
HOVERGEN	Q9N0F1.
Enzyme and pathway databases
BRENDA	2.3.1.61. 249.
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...

Entry information

Entry name

ODO2_PIG

Accession

Primary (citable) accession number: Q9N0F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)