ID A7THE3_VANPO Unreviewed; 1020 AA.
AC A7THE3;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, 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 ORFNames=Kpol_1039p16 {ECO:0000313|EMBL:EDO18267.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO18267.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480391; EDO18267.1; -; Genomic_DNA.
DR RefSeq; XP_001646125.1; XM_001646075.1.
DR AlphaFoldDB; A7THE3; -.
DR STRING; 436907.A7THE3; -.
DR GeneID; 5546544; -.
DR KEGG; vpo:Kpol_1039p16; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; A7THE3; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR PhylomeDB; A7THE3; -.
DR Proteomes; UP000000267; 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 Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 652..862
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1020 AA; 115290 MW; BFE2AE5E0DE07D09 CRC64;
MLRAISSVTS YSTSRRVLTN PALRNAPRLV KPLISSRRCL SSSTSSSDDF MSTVNSSYID
EMFEAWQKDP TSVHASWNAY FKNMKNLNVP ASKAFQSPPT LIGSPTGTES VPFGSGLSEN
VDENVRLHLK VQLLCRAYQV RGHLKAHIDP LKISFGDDKS KPVPSELTIQ YYGFTEKDLD
REINLGPGIL PRYARDGRTT MKLRDIISVM EKLYCSSYGI QYTHIPSKQK CEWLRERIEI
PNPFNYSVEQ KRQILDRLTW ATSFETFLST KFPNDKRFGL EGLESVVPGI KTLIDRAVEL
GVEDVVLGMA HRGRLNVLSN VVRKPNESIF SEFKGTSTRD DIEGSGDVKY HLGMNYQRPT
TSGKHVNLSL VANPSHLEAQ DPVVLGRTRA LLDAKDDLET KTKCIGVLLH GDAAFAGQGV
VYETMGFETL PAYSTGGTIH IITNNQIGFT TDPRFARSTP YPSDIAKTFD APIFHVNAND
VEAVTYIFNL AAEWRNTFHS DAIIDVVGWR KHGHNETDQP SFTQPLMYKE IAKQKSVIDV
YSEQLIKEGS FSEANINDLK TEVWEKFEEA FNKAKDYVPS QREWLTASWE NFKSPKELAT
EILPHNPTNV DLETLNGIGS AISSWPKGFE VHKNLKRILT NRGKSVDTGK GIDWSTGEAL
AYGSLVLEGY QVRVSGEDVE RGTFSQRHAV LHDQKSEAVY TPLKHLSKDQ GEFTISNSSL
SEYGVMGFEY GYSLTSPDYL VVWEAQFGDF ANTAQVIIDQ FIAGGEQKWK QRSGLVLSLP
HGYDGQGPEH SSGRLERFLQ LANEDPRYFP SELKLQRQHQ DCNFQVVYPT TPANLFHILR
RQQHRQFRKP LILFFSKQLL RHPLARSNIE EFTEGGFEWI IEDSEHGKTI ATKEETKRLV
LMTGQVYTAL HKRREELGDK STAFLRIEEL HPFPFAQLRD TLNSYPNLEE IVWCQEEPLN
MGSWGYVSPR LQTTLKETNN YKNHAVRYCG RNPSGAVAAG SKSLHLAEEE SFLKDVFNQS
//
