ID A0A0R0EA65_SOYBN Unreviewed; 978 AA.
AC A0A0R0EA65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Name=100816277 {ECO:0000313|EnsemblPlants:KRG90560};
GN ORFNames=GLYMA_20G099200 {ECO:0000313|EMBL:KRG90560.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG90560.1};
RN [1] {ECO:0000313|EMBL:KRG90560.1, ECO:0000313|EnsemblPlants:KRG90560}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG90560};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90560.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRG90560}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG90560};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG90560.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90560.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000853; KRG90560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0EA65; -.
DR EnsemblPlants; KRG90560; KRG90560; GLYMA_20G099200.
DR Gramene; KRG90560; KRG90560; GLYMA_20G099200.
DR Proteomes; UP000008827; Chromosome 20.
DR ExpressionAtlas; A0A0R0EA65; baseline and differential.
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; 2.
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:UP000008827};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 636..806
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 978 AA; 111026 MW; 2CF55F0326FE2E85 CRC64;
MAWFRVASSI VKHDAIRRNL YRGAKRTSTV LPSTSRIRKF HTTVVKSKEQ TAPVPRPVPL
SKLTDNFLDG TSSVYLEELQ RAWEADPDSV DESWDNFFRN FVGQASTSPG ISGQTIQESM
QLLLLVRAYQ VNGHMKAKLD PLGLEERKVP DELDPAFYGF TEADLDREFF LGVWKMSGFL
SENRPVQTLR FILSRLQQAY CGSIGYEYMH IPDREKCNWL RDRIETPTPT QYNRERREVI
FDRLAWSTLF ENFLATKWTS AKRFGLEGGE SVIPGMKEMF DRASDLGVES IVMGMAHRGR
LNVLGNVVRK PLRQIFCEFS GGQPADEVGL YTGTGDVKYH LGTSYDRPTR GGRRIHLSLV
ANPSHLEAVN PLVVGKTRAK QYYSNDVDRM KNMGVLIHGD GSFAGQGVVY ETLHLSALPN
YTTGGTIHIV FNNQVAFTTD PKSGRSSQYC TDVAKALNAP IFHVNGDDVE AVVHVCELAA
EWRQTFHSDV VVDFVCYRRF GHNEIDEPSF TQPKMYKVIR NHPSALEIYQ KKLLESGELT
QEDIDKIHKK VTSILNDEFL ASKDYVPKRR DWLSAYWSGF KSPEQISRIR NTGVKPEILK
SVGKAITILP KFFSPHKAVK RIYEQRAQMV ETGEDIDWGF AEALAFATLI VEGNHVRLSG
QDVERGTFSH RHAVVHDQTT GEIYCPLDHV IMNQNEEMFT VSNSSLSEFG VLGFELGYSM
ENPNSLVIWE AQFGDFANGA QVIFDNFLSS GESKWLRQTG LVVLLPHGYD GQGPEHSSGR
LERFLQIHRE FRKPLIVMSP KNLLRSKACR SNLSEFDDVQ GHPGFDKQGT RFKRLIKDQN
NHSDVEEGIR RLVLCSGKVY YELDEQRTKE DAKDVAICRV EQLCPFPYDL VQRELKRYPN
AEVVWCQEEP MNMGGYTYIL PRLISSMKAV GRGGYEDVKY VGRAPSAATA TGFLKVHLNE
QAELVQKAIQ REPINFPY
//
