ID   G0V9W9_NAUCC            Unreviewed;      1008 AA.
AC   G0V9W9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, 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   Name=NCAS0B06520 {ECO:0000313|EMBL:CCC68736.1};
GN   OrderedLocusNames=NCAS_0B06520 {ECO:0000313|EMBL:CCC68736.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC68736.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC68736.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) 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; HE576753; CCC68736.1; -; Genomic_DNA.
DR   RefSeq; XP_003675107.1; XM_003675059.1.
DR   AlphaFoldDB; G0V9W9; -.
DR   STRING; 1064592.G0V9W9; -.
DR   GeneID; 11526030; -.
DR   KEGG; ncs:NCAS_0B06520; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; G0V9W9; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000001640; Chromosome 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          641..851
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1008 AA;  113828 MW;  29F750686463A012 CRC64;
     MLRAISRPLY RHGSKSLIKS ALLKQYASKV TATRCLTTGS DTFLSTSNSS YIDEMYQAWQ
     KDPSSVHVSW DAYFKNMSNP KVAASNAFQA PPILVASLPG APSAHLSNSM DENVSLHLKV
     QLLCRAYQVR GHLKAHIDPL GLSFGDSKDK PVPPELTLDY YGFTEKDLDR EIILGPGILP
     RFAKNGKTTM KLRDIIADME SLYCSSYGIQ YTHIPSKVKC EWLRERIEIP KPYEYTIDQK
     RQILDRLTWA TSFETFLSTK FPNEKRFGLE GLEAVVPGIK TLIDRSVELG VEDVVLGMAH
     RGRLNVLSNV VRKPNESIFS EFQGTTTTNN IEGSGDVKYH LGMNYQRPTT SGKYVNLSLV
     ANPSHLEAQD PVVLGRTRAL LHAKGDLKNQ TKALGVLLHG DAAFAGQGVV YETMGFQTLP
     EYSTGGTIHV ITNNQIGFTT DPRFARSTPY PSDIAKAIDA PIFHCNANDI EAVTFIFNLA
     AEWRNEFHTD AIIDVVGWRK HGHNETDQPS FTQPLMYQKI AKQKSVIDEY TDKLIKEGSF
     TKSDIDEHKK WVWGLFEKAF EKSKDYVPTQ REWLTAAWED FKSPKELATE ILPHNPTNVS
     VDIIQDIGKA LSSWPENFEV HKNLKRILTN RGKSISTGEG IDWSTGEALA FGTLVLEGYN
     VRVSGEDVER GTFSQRHAVL HDQKSEDTYV PLKHLSAKQA DFSICNSSLS EYGVMGFEYG
     YSLTSPDYLV MWEAQFGDFA NTAQVITDQF IAGGEQKWKQ RSGLVLSLPH GYDGQGPEHS
     SGRLERFLQM ANEDPRYFPS EEKLQRQHQD CNYQVVYPTT PANLFHIIRR QQHRQFRKPL
     ILFFSKQLLR HPLARSQLEE FTEGGFQWII EDVEHGRAIG TKEETKRLVL LSGQVYTALH
     KKRETIGDKS TALMKIEELH PFPFAQLRDA IDSYPNLEEF VWCQEEPLNM GGWAYAAPRL
     QTTLQETQNY KNHTVRYCGR NPSGAVAAGS KSLHIAEEEA FLKDVFGQ
//