ODO2_YEAST
ID ODO2_YEAST Reviewed; 463 AA.
AC P19262; D6VSD1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=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=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE Flags: Precursor;
GN Name=KGD2; OrderedLocusNames=YDR148C; ORFNames=YD8358.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115121; DOI=10.1128/mcb.10.8.4221-4232.1990;
RA Repetto B., Tzagoloff A.;
RT "Structure and regulation of KGD2, the structural gene for yeast
RT dihydrolipoyl transsuccinylase.";
RL Mol. Cell. Biol. 10:4221-4232(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
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).
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 -!- INTERACTION:
CC P19262; P20967: KGD1; NbExp=6; IntAct=EBI-12464, EBI-12459;
CC P19262; P09624: LPD1; NbExp=4; IntAct=EBI-12464, EBI-5940;
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- INDUCTION: Transcriptionally regulated by glucose and activated by the
CC HAP2 and HAP3 proteins.
CC -!- MISCELLANEOUS: Present with 7970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M34531; AAA34720.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90371.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11991.1; -; Genomic_DNA.
DR PIR; S57975; XUBYSD.
DR RefSeq; NP_010432.3; NM_001180455.3.
DR AlphaFoldDB; P19262; -.
DR SMR; P19262; -.
DR BioGRID; 32202; 380.
DR ComplexPortal; CPX-1293; Mitochondrial 2-oxoglutarate dehydrogenase complex.
DR DIP; DIP-1102N; -.
DR IntAct; P19262; 50.
DR MINT; P19262; -.
DR STRING; 4932.YDR148C; -.
DR iPTMnet; P19262; -.
DR MaxQB; P19262; -.
DR PaxDb; P19262; -.
DR PRIDE; P19262; -.
DR EnsemblFungi; YDR148C_mRNA; YDR148C; YDR148C.
DR GeneID; 851726; -.
DR KEGG; sce:YDR148C; -.
DR SGD; S000002555; KGD2.
DR VEuPathDB; FungiDB:YDR148C; -.
DR eggNOG; KOG0559; Eukaryota.
DR GeneTree; ENSGT00930000151014; -.
DR HOGENOM; CLU_016733_0_1_1; -.
DR InParanoid; P19262; -.
DR OMA; MKVPSPG; -.
DR BioCyc; YEAST:YDR148C-MON; -.
DR BRENDA; 2.3.1.61; 984.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-71064; Lysine catabolism.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00868; UER00840.
DR PRO; PR:P19262; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P19262; protein.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; ISA:SGD.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:ComplexPortal.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acyltransferase; Lipoyl; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..463
FT /note="Dihydrolipoyllysine-residue succinyltransferase
FT component of 2-oxoglutarate dehydrogenase complex,
FT mitochondrial"
FT /id="PRO_0000020478"
FT DOMAIN 73..148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REPEAT 185..190
FT /note="1"
FT REPEAT 191..196
FT /note="2"
FT REPEAT 197..202
FT /note="3"
FT REPEAT 204..209
FT /note="4; approximate"
FT REGION 144..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..209
FT /note="4 X 6 AA approximate tandem repeats of A-[SP]-K-K-E-
FT [AV]"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /evidence="ECO:0000250"
FT MOD_RES 114
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT CONFLICT 170..208
FT /note="PSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKA -> HRKVSPQGK
FT TQVRKRLQRKKLLQRKKPLQRKKLQNQKRT (in Ref. 1; AAA34720)"
FT /evidence="ECO:0000305"
FT CONFLICT 441..445
FT /note="REAVT -> EKLLS (in Ref. 1; AAA34720)"
FT /evidence="ECO:0000305"
FT CONFLICT 460..463
FT /note="MLLW -> CCYGDLKFAAHTNLIS (in Ref. 1; AAA34720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50431 MW; C06FEB1DE385AE19 CRC64;
MLSRATRTAA AKSLVKSKVA RNVMAASFVK RHASTSLFKQ ANKVESLGSI YLSGKKISVA
ANPFSITSNR FKSTSIEVPP MAESLTEGSL KEYTKNVGDF IKEDELLATI ETDKIDIEVN
SPVSGTVTKL NFKPEDTVTV GEELAQVEPG EAPAEGSGES KPEPTEQAEP SQGVAARENS
SEETASKKEA APKKEAAPKK EVTEPKKADQ PKKTVSKAQE PPVASNSFTP FPRTETRVKM
NRMRLRIAER LKESQNTAAS LTTFNEVDMS ALMEMRKLYK DEIIKKTGTK FGFMGLFSKA
CTLAAKDIPA VNGAIEGDQI VYRDYTDISV AVATPKGLVT PVVRNAESLS VLDIENEIVR
LSHKARDGKL TLEDMTGGTF TISNGGVFGS LYGTPIINSP QTAVLGLHGV KERPVTVNGQ
IVSRPMMYLA LTYDHRLLDG REAVTFLKTV KELIEDPRKM LLW
