Reviewed, UniProtKB/Swiss-Prot O74378 (ODO1_SCHPO)

Names and origin

Protein names

Recommended name:
    2-oxoglutarate dehydrogenase E1 component, mitochondrial
    EC=1.2.4.2
Alternative name(s):
    Alpha-ketoglutarate dehydrogenase

Gene names

Name:	kgd1
ORF Names:	SPBC3H7.03c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	1009 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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 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 + CO(2).
Cofactor	Thiamine pyrophosphate By similarity.
Enzyme regulation	Catabolite repressed By similarity.
Subcellular location	Mitochondrion matrixBy similarity.
Sequence similarities	Belongs to the alpha-ketoglutarate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: InterPro thiamin 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 E1 component, mitochondrial		PRO_0000315629

Sequences

	Sequence		Length	Mass (Da)
	O74378-1 [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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[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: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA20299.1.
PIR	T40412.
RefSeq	NP_595772.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2540991.
KEGG	spo:SPBC3H7.03c.
NMPDR	fig|4896.1.peg.1638.
Organism-specific databases
GeneDB_Spombe	SPBC3H7.03c.
Gene expression databases
ArrayExpress	O74378.
Family and domain databases
InterPro	IPR011603. 2oxoglutarate_DHase_E1. IPR001017. DHase_E1. IPR005475. Transketo_Cen_R. [Graphical view]
PANTHER	PTHR23152. 2oxoglutarate_DH_E1. 1 hit.
Pfam	PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view]
PIRSF	PIRSF000157. Oxoglu_dh_E1. 1 hit.
TIGRFAMs	TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNet	Search...

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:	November 25, 2008
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)