Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Gene

kgd2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 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

Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei424 – 4241By similarity
Active sitei428 – 4281By similarity

GO - Molecular functioni

  1. dihydrolipoyllysine-residue succinyltransferase activity Source: PomBase

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: PomBase
  2. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
  3. tricarboxylic acid cycle Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
REACT_322076. Lysine catabolism.
UniPathwayiUPA00868; UER00840.

Names & Taxonomyi

Protein namesi
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 namesi
Name:kgd2
ORF Names:SPBC776.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

PomBaseiSPBC776.15c.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 452Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrialPRO_0000020477
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831N6-lipoyllysinePROSITE-ProRule annotation

Proteomic databases

MaxQBiO94681.
PaxDbiO94681.
PRIDEiO94681.

Interactioni

Protein-protein interaction databases

MINTiMINT-4686150.
STRINGi4896.SPBC776.15c-1.

Structurei

3D structure databases

ProteinModelPortaliO94681.
SMRiO94681. Positions 223-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 11776Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
InParanoidiO94681.
KOiK00658.
OMAiSERQEEH.
OrthoDBiEOG73V6W0.
PhylomeDBiO94681.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O94681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSYGNGFRM MAKCLLSLRS GYSVTAPVSK SMANVLWARY ASTRIKTPPF
60 70 80 90 100
PESITEGTLA QWLKQPGEYV NKDEEIASVE TDKIDAPVTA PDAGVLKEQL
110 120 130 140 150
VKEGDTITID QDIAVIDTSA APPEGGSAGP KKDEVKTADA DAAKDLSTPQ
160 170 180 190 200
DSSKPIEEKP MPDLGAEQKE SAPSSTKPAP DAKEPEFSSP KPKPAKSEPV
210 220 230 240 250
KQSKPKATET ARPSSFSRNE DRVKMNRMRL RIAERLKESQ NRAASLTTFN
260 270 280 290 300
ECDMSAVVAL RKKYKDEILK ETGVKIGFMS FFSKACTQAM KQIPAINGSI
310 320 330 340 350
EGEGKGDTLV YRDFCDLSIA VATPKGLVTP VIRNAESMSL LEIESAIATL
360 370 380 390 400
GSKARAGKLA IEDMASGTFT ISNGGIFGSL YGTPIINLPQ TAVLGLHAIK
410 420 430 440 450
ERPVVINGQV VPRPMMYLAL TYDHRMVDGR EAVTFLRLVK EYIEDPAKML

LV
Length:452
Mass (Da):48,964
Last modified:April 30, 1999 - v1
Checksum:iBAB03FB2842A37F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22888.1.
PIRiT40686.
RefSeqiNP_596331.1. NM_001022252.2.

Genome annotation databases

EnsemblFungiiSPBC776.15c.1; SPBC776.15c.1:pep; SPBC776.15c.
GeneIDi2541170.
KEGGispo:SPBC776.15c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22888.1.
PIRiT40686.
RefSeqiNP_596331.1. NM_001022252.2.

3D structure databases

ProteinModelPortaliO94681.
SMRiO94681. Positions 223-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4686150.
STRINGi4896.SPBC776.15c-1.

Proteomic databases

MaxQBiO94681.
PaxDbiO94681.
PRIDEiO94681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC776.15c.1; SPBC776.15c.1:pep; SPBC776.15c.
GeneIDi2541170.
KEGGispo:SPBC776.15c.

Organism-specific databases

PomBaseiSPBC776.15c.

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281563.
InParanoidiO94681.
KOiK00658.
OMAiSERQEEH.
OrthoDBiEOG73V6W0.
PhylomeDBiO94681.

Enzyme and pathway databases

UniPathwayiUPA00868; UER00840.
ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
REACT_322076. Lysine catabolism.

Miscellaneous databases

NextBioi20802282.
PROiO94681.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
InterProiIPR003016. 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]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01347. sucB. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiODO2_SCHPO
AccessioniPrimary (citable) accession number: O94681
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 2002
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 109 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.