ID K5WUG8_AGABU Unreviewed; 1012 AA.
AC K5WUG8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=AGABI1DRAFT_113697 {ECO:0000313|EMBL:EKM79066.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM79066.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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; JH971390; EKM79066.1; -; Genomic_DNA.
DR RefSeq; XP_007329833.1; XM_007329771.1.
DR AlphaFoldDB; K5WUG8; -.
DR STRING; 597362.K5WUG8; -.
DR GeneID; 18824081; -.
DR KEGG; abp:AGABI1DRAFT113697; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; K5WUG8; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000008493; 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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 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:UP000008493};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 639..849
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1012 AA; 114020 MW; 60E4AA0435EB1F7E CRC64;
MLSRRVVVGR LSTLARASRS LRPTPPPLIR RGYALARGPS HNDPFANGTN AYYADEMYRL
WRQDPKSVHT SWDVYFSGLD QGMPSHHAFQ PPPTTHLPHP ADGAPALHAG DGAELNDHLK
VQLLVRAYQV RGHHVAELDP LGILDTDLAD VRPPELELSR YGFTERDLEK DITLGPGILP
HFATEGNKTM KLKDIIRTLK RIYCGHVGIQ YVHIPDKEQC DWIRERVETP KPWNYTVEEK
RMILDRLIWS ESFEKFMASK YPNEKRFGLE GCEALVPGMK ALIDRSVETG VKHITMGMPH
RGRLNVLANV IRKPIEAILN EFSGDEDDNW PAGDVKYHLG ANYVRPTPSG KKVSLSLVAN
PSHLEAADPV VLGKTRAIQH FENDEIAHTT AMGVLLHGDA SFAGQGVVYE TMGLHSLPSY
GTGGTIHLIV NNQIGFTTDP RFARSTPYPS DIAKSIDAPI FHVNGDNVEA VNFVCQLAAD
YRAKFKKDVV IDIVCYRRYG HNETDQPSFT QPRMYEAIKN QPTPLTKYTK FLVGRGTFTE
KDIEEHKKWV WGMLETAANG AKDYVPTSKE WLSAAWTGFP SPRQLAEQAL PTRATGSDVP
TLRQIGKAIS TFPQGFTTHR NLARILNARG KTVEEGTNID WSTAEALAFG TLALEKIHVR
LSGQDVERGT FSQRHAVIHD QANEQQYVPL NDLGSNQARF VVCNSSLSEF GTLGFELGYS
LVSPDSLTIW EAQFGDFANN AQCIIDQFIA AGERKWLQRT GLVVSLPHGY DGQGPEHSSG
RIERFLQLCD DHPHIYPSPE KIERQHQDCN MQVVYPTTPA NYFHVLRRQI HRDFRKPLIV
FFSKSLLRHP KARSSLDEMV GETHFERYIP EASEDLVAPD QVKRHILCSG QVYYALLQAR
EERGIKDVAI SRIEQLSPFP YDMVTSHLDK YPNADLLWCQ EEPMNNGAWT YIGPRIYTAA
SRTQNHKGKY PYYAGREPTS SVATGSKTQH KKETEAFVNT AFDTWTEMHH LK
//