O94681 (ODO2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 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
Probable dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

Gene names

Name:	kgd2
ORF Names:	SPBC776.15c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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) By similarity.
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.
Subcellular location	Mitochondrion By similarity.
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: PomBase L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	mitochondrial nucleoid Inferred from sequence or structural similarity. Source: PomBase mitochondrial oxoglutarate dehydrogenase complex Inferred by curator. Source: PomBase
Molecular_function	dihydrolipoyllysine-residue succinyltransferase activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion
	Chain	? – 452		Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial		PRO_0000020477
Regions
	Domain	43 – 116	74	Lipoyl-binding
Sites
	Active site	424	1	By similarity
	Active site	428	1	By similarity
Amino acid modifications
	Modified residue	83	1	N6-lipoyllysine Potential

Sequences

	Sequence		Length	Mass (Da)
	O94681 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: BAB03FB2842A37F1	FASTA	452	48,964
	10 20 30 40 50 60 MTSYGNGFRM MAKCLLSLRS GYSVTAPVSK SMANVLWARY ASTRIKTPPF PESITEGTLA 70 80 90 100 110 120 QWLKQPGEYV NKDEEIASVE TDKIDAPVTA PDAGVLKEQL VKEGDTITID QDIAVIDTSA 130 140 150 160 170 180 APPEGGSAGP KKDEVKTADA DAAKDLSTPQ DSSKPIEEKP MPDLGAEQKE SAPSSTKPAP 190 200 210 220 230 240 DAKEPEFSSP KPKPAKSEPV KQSKPKATET ARPSSFSRNE DRVKMNRMRL RIAERLKESQ 250 260 270 280 290 300 NRAASLTTFN ECDMSAVVAL RKKYKDEILK ETGVKIGFMS FFSKACTQAM KQIPAINGSI 310 320 330 340 350 360 EGEGKGDTLV YRDFCDLSIA VATPKGLVTP VIRNAESMSL LEIESAIATL GSKARAGKLA 370 380 390 400 410 420 IEDMASGTFT ISNGGIFGSL YGTPIINLPQ TAVLGLHAIK ERPVVINGQV VPRPMMYLAL 430 440 450 TYDHRMVDGR EAVTFLRLVK EYIEDPAKML LV

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA22888.1.
PIR	T40686.
RefSeq	NP_596331.1. NM_001022252.2.
3D structure databases
ProteinModelPortal	O94681.
SMR	O94681. Positions 223-450.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPBC776.15c-1.
Proteomic databases
PaxDb	O94681.
PRIDE	O94681.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC776.15c.1; SPBC776.15c.1:pep; SPBC776.15c.
GeneID	2541170.
KEGG	spo:SPBC776.15c.
Organism-specific databases
PomBase	SPBC776.15c.
Phylogenomic databases
eggNOG	COG0508.
HOGENOM	HOG000281563.
KO	K00658.
OMA	VNADNEI.
OrthoDB	EOG483HD4.
Enzyme and pathway databases
UniPathway	UPA00868; UER00840.
Family and domain databases
Gene3D	3.30.559.10. 1 hit.
InterPro	IPR003016. 2-oxoA_DH_lipoyl-BS. IPR001078. 2-oxoacid_DH_actylTfrase. IPR000089. Biotin_lipoyl. IPR023213. CAT-like_dom. IPR011053. Single_hybrid_motif. IPR006255. SucB. [Graphical view]
Pfam	PF00198. 2-oxoacid_dh. 1 hit. PF00364. Biotin_lipoyl. 1 hit. [Graphical view]
SUPFAM	SSF51230. Hybrid_motif. 1 hit.
TIGRFAMs	TIGR01347. sucB. 1 hit.
PROSITE	PS50968. BIOTINYL_LIPOYL. 1 hit. PS00189. LIPOYL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20802282.

Entry information

Entry name

ODO2_SCHPO

Accession

Primary (citable) accession number: O94681

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program