ID A0A074YPN8_AURSE Unreviewed; 1048 AA.
AC A0A074YPN8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AUEXF2481DRAFT_65009 {ECO:0000313|EMBL:KEQ96042.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ96042.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ96042.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ96042.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584757; KEQ96042.1; -; Genomic_DNA.
DR RefSeq; XP_013344668.1; XM_013489214.1.
DR AlphaFoldDB; A0A074YPN8; -.
DR STRING; 1043005.A0A074YPN8; -.
DR GeneID; 25370020; -.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; A0A074YPN8; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000030641; 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:UP000030641};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 669..879
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1048 AA; 117949 MW; EDF98F30FD694A6C CRC64;
MLRASFSQCG KRLAAAGSRT NFSTISRSRP VVALTQSRRD LALSQFRSYA VAAEDTNKGV
DPNDSFLQGN TANYIDEMYM EWKRDPKSVH ISWQVYFRNM EKGDMPVSQA FQPPPTIIPA
PEGGAPGFSP TAAAGVGDSS DLTNHLKVQL LVRAYQARGH HKAKIDPLGI RNEASQFGYG
NPPELSLDHY NFTEADMEQE FSLGPGILPR FATEGQNKMK LKDIIAACER LYCGSYGIEY
IHIPDREQCD WLRARIEVPQ PYKYSVDEKR RILDRLIWSS SFESFLATKY PNDKRFGLEG
GESLIPGMKA LIDRSVDYGV KDIVIGMPHR GRLNVLSNVV RKPNESIFSE FAGSAEPADE
GSGDVKYHLG MNFERPTPSG KRVQLSLVAN PSHLEAEDPV VLGKTRAILH YNGDEKEANS
AMGVLLHGDA AFAGQGIVYE TMGFYALPSY QTGGTIHIVV NNQIGFTTDP RFSRSTPYCS
DIAKAIDAPV FHVNGDDVEA VNFVCQLAAD WRAEFKKDVV IDIVCYRKQG HNETDQPSFT
QPLMYKRISE QKPTLDKYIN QLIEDKTFTQ DDVEEHKKWV WGMLEESFSR SKDYQPTAKE
WLTSAWNGFK SPKELATEVL PHLPTAVETD TLKHIGEKIG TPPDGFNVHR NLKRILNNRT
KTINEGKNID MSTAEALAFG SLCMEGHHVR VSGQDVERGT FSQRHAVVHD QESESTYTPL
QDLGKDQGSF VVSNSSLSEF GVLGFEYGYS LSSPSALVMW EAQFGDFANN AQCIIDQFIA
SGEVKWLQRS GLVMSMPHGY DGQGPEHSSG RMERFLQLCN EDPRIFPAPN KLDRQHQDCN
MQIAYCTTPA NLFHILRRQM NRQFRKPLIL FFSKSLLRHP LARSSIEEFT GDSHFQWIIP
DPAHTEGEHQ IQPKEEIERV ILCTGQVYAA LHKYRQQNGI TNTAITRIEQ LNPFPWAQLK
ENLDSYPNAK NIVWAQEEPL NAGSWTFTQP RIETLLNETE HHNRRHVLYA GRNPSASVAT
GLKSSHMKEE QDLLDTAFNV KQDKLKGE
//
