ID   ODO2_SCHPO              Reviewed;         452 AA.
AC   O94681;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial;
DE            EC=2.3.1.61;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE            Short=OGDC-E2;
DE   AltName: Full=Probable dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE   Flags: Precursor;
GN   Name=kgd2; ORFNames=SPBC776.15c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC         Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC       Note=Binds 1 lipoyl cofactor covalently.;
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA22888.1; -; Genomic_DNA.
DR   PIR; T40686; T40686.
DR   RefSeq; NP_596331.1; NM_001022252.2.
DR   AlphaFoldDB; O94681; -.
DR   SMR; O94681; -.
DR   BioGRID; 277684; 2.
DR   STRING; 4896.SPBC776.15c.1; -.
DR   MaxQB; O94681; -.
DR   PaxDb; O94681; -.
DR   PRIDE; O94681; -.
DR   EnsemblFungi; SPBC776.15c.1; SPBC776.15c.1:pep; SPBC776.15c.
DR   GeneID; 2541170; -.
DR   KEGG; spo:SPBC776.15c; -.
DR   PomBase; SPBC776.15c; kgd2.
DR   VEuPathDB; FungiDB:SPBC776.15c; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   HOGENOM; CLU_016733_0_1_1; -.
DR   InParanoid; O94681; -.
DR   OMA; MKVPSPG; -.
DR   PhylomeDB; O94681; -.
DR   Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-SPO-71064; Lysine catabolism.
DR   Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00868; UER00840.
DR   PRO; PR:O94681; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:PomBase.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; ISS:PomBase.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:PomBase.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipoyl; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..452
FT                   /note="Probable dihydrolipoyllysine-residue
FT                   succinyltransferase component of 2-oxoglutarate
FT                   dehydrogenase complex, mitochondrial"
FT                   /id="PRO_0000020477"
FT   DOMAIN          42..117
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          119..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        424
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   452 AA;  48964 MW;  BAB03FB2842A37F1 CRC64;
     MTSYGNGFRM MAKCLLSLRS GYSVTAPVSK SMANVLWARY ASTRIKTPPF PESITEGTLA
     QWLKQPGEYV NKDEEIASVE TDKIDAPVTA PDAGVLKEQL VKEGDTITID QDIAVIDTSA
     APPEGGSAGP KKDEVKTADA DAAKDLSTPQ DSSKPIEEKP MPDLGAEQKE SAPSSTKPAP
     DAKEPEFSSP KPKPAKSEPV KQSKPKATET ARPSSFSRNE DRVKMNRMRL RIAERLKESQ
     NRAASLTTFN ECDMSAVVAL RKKYKDEILK ETGVKIGFMS FFSKACTQAM KQIPAINGSI
     EGEGKGDTLV YRDFCDLSIA VATPKGLVTP VIRNAESMSL LEIESAIATL GSKARAGKLA
     IEDMASGTFT ISNGGIFGSL YGTPIINLPQ TAVLGLHAIK ERPVVINGQV VPRPMMYLAL
     TYDHRMVDGR EAVTFLRLVK EYIEDPAKML LV