ID   B3LTX2_YEAS1            Unreviewed;      1014 AA.
AC   B3LTX2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN   ORFNames=SCRG_05297 {ECO:0000313|EMBL:EDV09603.1};
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV09603.1, ECO:0000313|Proteomes:UP000008335};
RN   [1] {ECO:0000313|Proteomes:UP000008335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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DR   EMBL; CH408055; EDV09603.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LTX2; -.
DR   SMR; B3LTX2; -.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          646..856
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1014 AA;  114417 MW;  F399BC58B8F6B1CB CRC64;
     MLRFVSSQTC RYSSRGLLKT SLLKNASTVK IVGRGLATTG TDNFLSTSNA TYIDEMYQAW
     QKDPSSVHVS WDAYFKNMSN PKIPATKAFQ APPSISNFPQ GTEAAPLGTA MTGSVDENVS
     IHLKVQLLCR AYQVRGHLKA HIDPLGISFG SNKNNPVPPE LTLDYYGFSK HDLDKEINLG
     PGILPRFARD GKSKMSLKEI VDHLEKLYCS SYGVQYTHIP SKQKCDWLRE RIEIPEPYQY
     TVDQKRQILD RLTWATSFES FLSTKFPNDK RFGLEGLESV VPGIKTLVDR SVELGVEDIV
     LGMAHRGRLN VLSNVVRKPN ESIFSEFKGS SARDDIEGSG DVKYHLGMNY QRPTTSGKYV
     NLSLVANPSH LESQDPVVLG RTRALLHAKN DLKEKTKALG VLLHGDAAFA GQGVVYETMG
     FLTLPEYSTG GTIHVITNNQ IGFTTDPRFA RSTPYPSDLA KAIDAPIFHV NANDVEAVTF
     IFNLAAEWRH KFHTDAIIDV VGWRKHGHNE TDQPSFTQPL MYKKIAKQKS VIDVYTEKLI
     SEGTFSKKDI DEHKKWVWNL FEDAFEKAKD YVPSQREWLT AAWEGFKSPK ELATEILPHE
     PTNVPESTLK ELGKVLSSWP EGFEVHKNLK RILKNRGKSI ETGEGIDWAT GEALAFGTLV
     LDGQNVRVSG EDVERGTFSQ RHAVLHDQQS EAIYTPLSTL NNEKADFTIA NSSLSEYGVM
     GFEYGYSLTS PDYLVMWEAQ FGDFANTAQV IIDQFIAGGE QKWKQRSGLV LSLPHGYDGQ
     GPEHSSGRLE RFLQLANEDP RYFPSEEKLQ RQHQDCNFQV VYPTTPANLF HILRRQQHRQ
     FRKPLALFFS KQLLRHPLAR SSLSEFTEGG FQWIIEDIEH GKSIGTKEET KRLVLLSGQV
     YTALHKRRES LGDKTTAFLK IEELHPFPFA QLRDSLNSYP NLEEIVWCQE EPLNMGSWAY
     TEPRLHTTLK ETDKYKDFKV RYCGRNPSGA VAAGSKSLHL AEEDAFLKDV FQQS
//