ID C4QZL6_KOMPG Unreviewed; 1001 AA.
AC C4QZL6;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=PAS_chr2-1_0089 {ECO:0000313|EMBL:CAY68690.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY68690.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY68690.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY68690.1; -; Genomic_DNA.
DR RefSeq; XP_002490970.1; XM_002490925.1.
DR AlphaFoldDB; C4QZL6; -.
DR SMR; C4QZL6; -.
DR STRING; 644223.C4QZL6; -.
DR EnsemblFungi; CAY68690; CAY68690; PAS_chr2-1_0089.
DR GeneID; 8198485; -.
DR KEGG; ppa:PAS_chr2-1_0089; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; C4QZL6; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000000314; 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:UP000000314};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 631..841
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1001 AA; 112771 MW; E45D4B6092888EB5 CRC64;
MLKSFKGISS RSSILRNAPR RLIQTRLLAT DSFLQSNNAN YIDEMYEQWS KDPSSVHSSW
NAYFKNLDQG VPPSRAFQAP PTLIPQPAGG IPNLVPVGNA SGNSNVLTHL KAQLLVRAYQ
VRGHQKAKID PLGISFGDDK SKPVPKELTQ EFYGFTEADL DTEITLGPGI LPKFAEAGHP
TMKLRDIIKA CEKIYCSSYG VEYVHIPSRE KCDWLRERIE IPTPYKYSVD EKRQILDRLI
WSCSFENFLS SKFPNDKRFG VEGAESVIPG MKALIDTAVE NGVEDVVIGM AHRGRLNMLS
NVVRKPNESI FSEFTGSKDF DEGSGDVKYH LGMNYVRPTT SGKKVHLSLV ANPSHLEAED
PVVLGRTRAI QHYKGDVGEF NKAMGILVHG DAAFAGQGIV YETMGFAALP AYSTGGTIHI
IINNQIGFTT DPRFARSTPY PSDIAKSINA PILHVNADDV ESVIFNFQLA AEWRQTFHSD
VILDVVGYRK YGHNETDQPS FTQPLMYQKI AEKKQVLDIY VDKLIKEGSF TLDDINEHKQ
WVWNTLEEAF TKSVEYKPTS REWLTTPWEG FKSPKELASE VLPHLPTSVE RGVVERIGDT
ISSWPEGFEV HRNLKRILKN RKDSIQKGEG IDWSTGEALA FGSLVIEGYH VRISGQDVER
GTFSQRHAVL HDQNSEKVYI PLKHLSKVQS DFGISNSSLS EYGCMGFEYG YSLTSPDALV
MWEAQFGDFA NTAQVIIDQF LAAGESKWKQ RSGVVLSLPH GYDGQGSEHS SARLERYLQL
CNEDPRVYPS PEKLERQHQD CNMQVAYPTT PANLFHLLRR QMHRQFRKPL ILLFSKKLLR
HPLARSNIED FIGESSFQWI IEDSELGKTI NDKEGIKRLV LCSGQVHSSL HKKRADIGDK
ETAVLKIEQL HPFPFEQLKN AIDSYPSLDE IVWCQEEPLN MGSYAFSAPR IVTVLEQTEK
YKDYNLRYAG RNPAAAVAVG TKSMHVAQEE AFLDDVFQIQ N
//
