ID   A3LZW8_PICST            Unreviewed;      1015 AA.
AC   A3LZW8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 87.
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=KGD1 {ECO:0000313|EMBL:ABN68415.2};
GN   ORFNames=PICST_79721 {ECO:0000313|EMBL:ABN68415.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68415.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN68415.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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). {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; CP000502; ABN68415.2; -; Genomic_DNA.
DR   RefSeq; XP_001386444.2; XM_001386407.1.
DR   AlphaFoldDB; A3LZW8; -.
DR   SMR; A3LZW8; -.
DR   STRING; 322104.A3LZW8; -.
DR   GeneID; 4840878; -.
DR   KEGG; pic:PICST_79721; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   InParanoid; A3LZW8; -.
DR   OMA; RDSYCRT; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000002258; Chromosome 8.
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   ECO:0000313|EMBL:ABN68415.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          647..857
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1015 AA;  114107 MW;  4094E124207E0011 CRC64;
     MLKAFRNVVP RGQLLRASAR PSLRSMAPLT SSTSIRSTNS IRCFATGTDS FLQGNNSNYI
     DEMYDAWRQD PSSVHASWNA YFKNIESSNI PPSQAFQAPP TIVPTVSGGA AGFVPGSNPI
     SEDVVTHLKV QLLVRAYQVR GHQKAKIDPL GISFGDNSDT PKELTLDYYG FTDVDLNKQI
     TLGPGILPRF AEAGKKSLTL REIIENCEKL YCQSYGVEYV HIPSKEQCDW LRERIEIPQP
     FKYSADQKRQ ILDRLIWSCS FESFLATKFP NDKRFGLEGA EAVVPGMKAL IDTSVEFGVE
     DIVIGMPHRG RLNMLSNVVR KPNESIFSEF TGSKEFDEGS GDVKYHLGMN YARPTTSGKF
     VNLSIVANPS HLEAEDGVVL GKTRAIQQYK NDIGDYKRAM PILLHGDAAF AGQGVVYETM
     GFAHLPAYST GGTIHIIVNN QIGFTTDPRY SRSTLYPSDI AKASNSPIFH VNADDVEACI
     FVFNLAAEWR ATFHSDVIID VVGYRKHGHN ETDQPAFTQP LMYKKIAEKK SVLEYYTNQL
     IQEGTFTTED ISEHKKWVWN LLEDYFAKSK EYVPTSREWL TTPWEDFKSP KELATEVLPH
     LPTAVDEETL KKIGKAISEA PEGFEIHRNL KRILNTRNKT VETGEGIDWA TGEALAFGTL
     ALEGYHVRVS GQDVERGTFS QRHAVLHDQQ SEKTYTPLNH LSEEQGAFVI SNSSLSEYGV
     LGFEYGYSLT SPDALVQWEA QFGDFANTGQ VIMDQFIASA ESKWKQRSGL VLSLPHGYDG
     QGPEHSSGRI ERYLQMCNED QRYFPSPSKL ERQHQDCNFQ VAYPTTPANL FHLLRRQMHR
     QFRKPLALFF SKSLLRHPLA RSDLSEFTND SHFQWIIEDA EYGKTIAPKE EIKRVVLCSG
     QVFTALHKKR AAIEDKTTAF IKIEQVHPFP FAQLRDALDS HPNLEDLVWC QEEPLNMGSY
     SFVSPRITTT LAETENHKGL TLRYAGRDPS ASVAAGSKAM HTAQEEAFLN ETFQV
//