ID A0A1E5RM91_9ASCO Unreviewed; 1025 AA.
AC A0A1E5RM91;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=AWRI3578_g2273 {ECO:0000313|EMBL:OEJ88029.1};
OS Hanseniaspora opuntiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=211096 {ECO:0000313|EMBL:OEJ88029.1, ECO:0000313|Proteomes:UP000095605};
RN [1] {ECO:0000313|Proteomes:UP000095605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3578 {ECO:0000313|Proteomes:UP000095605};
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:OEJ88029.1}.
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DR EMBL; LPNL01000004; OEJ88029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5RM91; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000095605; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 658..868
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1025 AA; 115954 MW; D71385516EE52229 CRC64;
MLSQKAIIIS KRCLSQKLAL NKSAAFQKTA GLVSSTKQVL INKQSRAYAS DDLFMSTSNA
AYIDEMYESW VRDPSSVHAS WNAYFKNMKN PHIPASKAFQ APPLQSVSVG TSYLEPKATI
SNAREDSNDP ALLLHLKAQL LCRAYQVRGH LQAHIDPLGI SFADDKTKKI PKELTLEHYG
FTEQDLDTEI SLGPGILPYF AATKPKMTLR ELVTNLKKTY SSSYGIEYTH IPSQEKCEWL
RTKVEIPKPY QYNIDEKKQI LDRLTWATQF ETFLSTKFPN DKRFGLEGLE GVVPGIKTLI
DRAVELGIED VILGMAHRGR LNVLSNVVRK PNESIFSEFK GSAPTDEYEG SGDVKYHLGM
NYKRPTTSGK FVNLSLVANP SHLESQDGVV LGRTRSIQHY KGDANDHKKA LPVLLHGDSA
FAGQGVVYET MGLTQLPKYS TGGTIHVITN NQIGFTTDPR FARSTPYPSD IAKAFNAPVF
HVNANDIEAV TFVFNLAAEY RQTFHTDVII DVVGWRKHGH NETDQPSFTQ PFMYQRIAKQ
KNVLDVYTEK LIAEGSFATE EIDAHKKWVW EMFETAFEKG KEYKPTSREW LTAPWEGFKS
PKELATEILP HEPTKVDEET LKRIGKQISS WPNGFEVHKN LKRILQNRGK AVETGEGIDW
STGEALAFGS LLLEGYHVRV SGQDVERGTF SQRHAVLHDQ KSENVYIPLQ RLTEDAEDFS
ISNSSLSEYG VLAFEYGYSL TSPNALVMWE AQFGDFANTA QVMIDQFIAG AEQKWKQRTG
LVLSLPHGYD GQGPEHSSGR IERFLQLADE DSRYFPSEQK LQRQHQDCNF QVAYPTTPAN
LFHLLRRQQH RQFRKPLAIL FSKQLLRHPL AKSKLSEFSE GSFKWIIEED DLIESGKLES
KENIKKVILL SGQVYTALHK KREDLGNKDT TFIKIEQMHP FPFKELKEAL DSYPNLEKIV
WCQEEPMNMG CWSYVEPRLK VVLGETKYAD VAPIYAGRDP SGSVAAGNKP LHVAQEQEFL
EKAFS
//
