ID   A0A1E5RNR7_9ASCO        Unreviewed;      1043 AA.
AC   A0A1E5RNR7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=AWRI3579_g803 {ECO:0000313|EMBL:OEJ88524.1};
OS   Hanseniaspora osmophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ88524.1, ECO:0000313|Proteomes:UP000095728};
RN   [1] {ECO:0000313|Proteomes:UP000095728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEJ88524.1}.
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DR   EMBL; LPNM01000005; OEJ88524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5RNR7; -.
DR   STRING; 56408.A0A1E5RNR7; -.
DR   InParanoid; A0A1E5RNR7; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000095728; 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:UP000095728};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          676..886
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1043 AA;  117956 MW;  4545E41732B8FD6F CRC64;
     MLRTLGKAAY FKSCTNCERV GTHIVNKYSS KHVYVKNYAR ILSTSRTLAQ KQQPSSSSSA
     DNFLQTSNAA YIDEMYESWQ HDPSSVHASW NAYFKNMNNM DIPASKAFVA PPASALGSSS
     NTSVAVGPTS LEFESTIENA TASHADPTVL LHLKIQLLCR AYQVRGHQKA HIDPLGIAFG
     DDKSKKLPEE LTLEHYGFTE KDLDTEVTLG PGILPRFAKM SPKMSIRDII ANLERLYCSS
     YGIEYVHIQS KKQCEWLRER IEVPKPFNYS IDEKRQILDR LTWATSFESF LSTKFPNDKR
     FGLEGLEGVV PGIKTLIDRS VEMGIDDVVL GMAHRGRLNV LSNVVRKPNE SIFSEFKGLK
     QDENEYEGSG DVKYHLGMNY QRPTTSGKFV NLSLVANPSH LESQDPVVLG RTRAIQHYKG
     DADDHKKAMG VLLHGDSAFA GQGVVYETMG FANLPKYSTG GTVHVITNNQ IGFTTDPRMA
     RSTLYPSDIA KAIDAPVFHV NANDIEAVTF VFNLAAEWRA TFHHDVIIDV VGWRKHGHNE
     TDQPLFTQPL MYHKIAKQKT VIEAYTEKLL NEGSFSKKEI DEHKAWVWGL FEQAFEKAKE
     YKPTSREWLT APWEGFKSPR ELATEILPHE PTNVDEETLK RIGKVISSWP ENFEVHKNLK
     RILQNRGKSV DKGEGIDWST GEALAFGTLL LEGYHVRVSG QDVERGTFSQ RHAVLHDQKS
     ENTYTPLQRL SEDHEKFSIS NSSLSEYGVL GFEYGYSLTS PNALVMWEAQ FGDFANTAQV
     IIDQFIAGAE SKWKQRSGLV LSLPHGYDGQ GPEHSSARLE RYLQLTNEDS RVFPDEEKLQ
     RQHQDCNFQV AYPTTPANLF HLLRRQQHRQ FRKPLVLLFS KQLLRHPLAR SSLSEFTEGS
     FQWIIEDPEL GKAIENKEGI ERLVLLTGQV YTALHKKRQE LENKTTAFLK IEQLNPFPFE
     LLKNAFNSYP NLKEIVWCQE EPLNMGGWSH ASPRLETVLK ETDNYKDTVI RFCGRDPSAS
     VAAGNKTLHL VQEAAFLKDV FGA
//