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Protein

2-oxoglutarate dehydrogenase, mitochondrial

Gene

kgd1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

Catabolite repressed.By similarity

GO - Molecular functioni

  1. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: GO_Central
  2. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: PomBase
  2. tricarboxylic acid cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_208292. Lysine catabolism.
REACT_213505. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
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 namesi
Name:kgd1
ORF Names:SPBC3H7.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC3H7.03c.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial nucleoid Source: PomBase
  2. mitochondrial oxoglutarate dehydrogenase complex Source: PomBase
  3. mitochondrion Source: PomBase
  4. oxoglutarate dehydrogenase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionSequence AnalysisAdd
BLAST
Chaini40 – 10099702-oxoglutarate dehydrogenase, mitochondrialPRO_0000315629Add
BLAST

Proteomic databases

MaxQBiO74378.
PaxDbiO74378.
PRIDEiO74378.

Interactioni

Protein-protein interaction databases

BioGridi277507. 1 interaction.
MINTiMINT-4678582.
STRINGi4896.SPBC3H7.03c-1.

Structurei

3D structure databases

ProteinModelPortaliO74378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
InParanoidiO74378.
KOiK00164.
OMAiKEYNKDR.
OrthoDBiEOG72G1GM.
PhylomeDBiO74378.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O74378-1 [UniParc]FASTAAdd to Basket

« Hide

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

EQFLNDALL
Length:1,009
Mass (Da):114,164
Last modified:November 1, 1998 - v1
Checksum:i4CB2598CE2B5E6AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20299.1.
PIRiT40412.
RefSeqiNP_595772.1. NM_001021673.2.

Genome annotation databases

EnsemblFungiiSPBC3H7.03c.1; SPBC3H7.03c.1:pep; SPBC3H7.03c.
GeneIDi2540991.
KEGGispo:SPBC3H7.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA20299.1.
PIRiT40412.
RefSeqiNP_595772.1. NM_001021673.2.

3D structure databases

ProteinModelPortaliO74378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277507. 1 interaction.
MINTiMINT-4678582.
STRINGi4896.SPBC3H7.03c-1.

Proteomic databases

MaxQBiO74378.
PaxDbiO74378.
PRIDEiO74378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3H7.03c.1; SPBC3H7.03c.1:pep; SPBC3H7.03c.
GeneIDi2540991.
KEGGispo:SPBC3H7.03c.

Organism-specific databases

PomBaseiSPBC3H7.03c.

Phylogenomic databases

eggNOGiCOG0567.
HOGENOMiHOG000259586.
InParanoidiO74378.
KOiK00164.
OMAiKEYNKDR.
OrthoDBiEOG72G1GM.
PhylomeDBiO74378.

Enzyme and pathway databases

ReactomeiREACT_208292. Lysine catabolism.
REACT_213505. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20802106.
PROiO74378.

Family and domain databases

Gene3Di3.40.50.970. 2 hits.
InterProiIPR011603. 2oxoglutarate_DH_E1.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiODO1_SCHPO
AccessioniPrimary (citable) accession number: O74378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 1, 1998
Last modified: February 4, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.