O74378 (ODO1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2-oxoglutarate dehydrogenase, mitochondrial
EC=1.2.4.2

Alternative name(s):
2-oxoglutarate dehydrogenase complex component E1
Short name=OGDC-E1
Alpha-ketoglutarate dehydrogenase

Gene names

Name:	kgd1
ORF Names:	SPBC3H7.03c

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	1009 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	2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.
Cofactor	Thiamine pyrophosphate By similarity.
Enzyme regulation	Catabolite repressed By similarity.
Subcellular location	Mitochondrion matrix By similarity Ref.2.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: PomBase 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 from sequence or structural similarity. Source: PomBase
Molecular_function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion Potential
	Chain	40 – 1009	970	2-oxoglutarate dehydrogenase, mitochondrial		PRO_0000315629

Sequences

	Sequence		Length	Mass (Da)
	O74378 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 4CB2598CE2B5E6AB	FASTA	1,009	114,164
	10 20 30 40 50 60 MLRFIPSSAK ARALRRSAVT AYRLNRLTCL SSLQQNRTFA TQPTDDFLTG GAADYVDEMY 70 80 90 100 110 120 DAWKKDPNSV HASWQAYFKN VQERGVSPSK AFQAPPLLDY ADSYTALDSS LINGNNYADI 130 140 150 160 170 180 DVGIYMKVQL LVRAYQSRGH HLAKLDPLGI NVNHNRPSEL TLEHYGFTES DLNRTIHLGP 190 200 210 220 230 240 GILPNFREAG RKTMTLREIV ETCEKIYCGS FAVEFTHISS RKRSNWILSH LETPTPFRYS 250 260 270 280 290 300 HDQKIMIFDR LSWADSFERF LFTKFPNDKR FGLEGCEAMV PGMKALIDRS VDEGISNIVI 310 320 330 340 350 360 GMAHRGRLNL LHNIVRKPAQ AIFSEFRGTQ DPDDEGSGDV KYHLGMNYQR PTPSGKRVSL 370 380 390 400 410 420 SLVANPSHLE AEDPVVLGKV RAIQHYTSDE ASHEQSMGIL IHGDAAFAAQ GVVYETFGLH 430 440 450 460 470 480 ALPGYSTGGT VHIVINNQIG FTTDPRFARS TPYCTDIAKS MEAPIFHVNG DDVEAVTFIC 490 500 510 520 530 540 QLAADWRKAF KTDVVVDIVC YRRHGHNETD QPSFTQPRMY KAIAKHPPTF KIYTQQLLQE 550 560 570 580 590 600 KTVSKAEVDA QEKRVWDILE SSFESSKNYK SDHREWLSNP WVGFASPKDL MTKILPSYPT 610 620 630 640 650 660 GVNIDTLKQI GKALYTLPEG FDAHRNLKRI LNNRNKSISS GEGIDMPTAE ALAFGTLLEE 670 680 690 700 710 720 GHHVRVSGQD VERGTFSQRH AVLHDQSSEN VYIPLNHLSP NQASFVIRNS SLSEYGVLGF 730 740 750 760 770 780 EYGYSLSSPN ALVVWEAQFG DFANNAQCII DQFIAAGETK WLQRTGIVLS LPHGYDGQGP 790 800 810 820 830 840 EHSSARMERY LQLCNEDPRE FPSEEKLQRQ HQDCNIQAIY VTKPSQYFHA LRRNIHRQFR 850 860 870 880 890 900 KPLVIFFSKS LLRHPAARST IDEFDEKHGF KLILEEEEHG KSILPPEKIE KLIICSGQVW 910 920 930 940 950 960 VALSKAREEN KIDNIAITRV EQLHPFGWKQ MAANISQYPN LKEIIWCQEE PLNAGAWTYM 970 980 990 1000 EPRIYTILKH LGRDLPVRYA GRPPSASVAA GNKQQHLAEQ EQFLNDALL

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.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA20299.1.
PIR	T40412.
RefSeq	NP_595772.1. NM_001021673.2.
3D structure databases
ProteinModelPortal	O74378.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4678582.
STRING	4896.SPBC3H7.03c-1.
Proteomic databases
PaxDb	O74378.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC3H7.03c.1; SPBC3H7.03c.1:pep; SPBC3H7.03c.
GeneID	2540991.
KEGG	spo:SPBC3H7.03c.
Organism-specific databases
PomBase	SPBC3H7.03c.
Phylogenomic databases
eggNOG	COG0567.
HOGENOM	HOG000259586.
KO	K00164.
OMA	IIKRGGA.
OrthoDB	EOG4GF6P6.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view]
PANTHER	PTHR23152. PTHR23152. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...
Other
NextBio	20802106.

Entry information

Entry name

ODO1_SCHPO

Accession

Primary (citable) accession number: O74378

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 1, 1998
Last modified:	May 29, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program