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Database: UniProt/TrEMBL
Entry: K5WUG8_AGABU
LinkDB: K5WUG8_AGABU
Original site: K5WUG8_AGABU 
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
//
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