ID A0A1D6J5Q3_MAIZE Unreviewed; 904 AA.
AC A0A1D6J5Q3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:AQK43259.1};
GN ORFNames=ZEAMMB73_Zm00001d025240 {ECO:0000313|EMBL:AQK43259.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK43259.1};
RN [1] {ECO:0000313|EMBL:AQK43259.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK43259.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; CM000786; AQK43259.1; -; Genomic_DNA.
DR EMBL; CM000786; AQK43273.1; -; Genomic_DNA.
DR EMBL; CM000786; AQK43274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6J5Q3; -.
DR OMA; HERINRW; -.
DR ExpressionAtlas; A0A1D6J5Q3; 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; 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; 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 519..732
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 904 AA; 103196 MW; 4BB05736C383535F CRC64;
MRLLLLVRAY QVSGHLKAKL DPLGLEERPV PDVLDPAFYG FSEADLDREF FLGVWMMAGF
LSENRPVQTL RSVLERLEQA YCGTIGYEYM HIPDREKCNW LRDRIETVNP MDYTYDRRQV
MLDRLIWSTQ FESFLATKWT TAKRFGLEGA ETLIPGMKEM FDRAAHLGVE SIVIGMPHRG
RLNVLGNVVR KPLRQIFSEF SGGTKPVNEG EGLYTGTGDV KYHLGTSYDR PTRGGKHIHL
SLVANPSHLE AVDPVVAGKT RAKQYYSNDR DRTKNLGVLL HGDGSFSGQG VVYETLHLSA
LENYTTGGTI HIVVNNQVAF TTDPRSGRSS QYCTDVAKAL DAPIFHVNGD DLEAVVHVCE
LAAEWRQTFH SDVVVDIVCY RRFGHNEIDE PSFTQPKMYK VIRNHPSALE IYQRKLLESG
KISKEDIDRL NKKVSTILNE EFQNSKDYVP NKRDWLSAYW TGFKSPEQIS RIRNTGVKPE
ILKRVGEAMT TLPENFKPHR AVKKIFDLRR QMIETGEGID WAVGEALAFA TLIIEGNHVR
LSGQDVERGT FSHRHSVIHD QETGEQYCPL DHLVMNQDAE LFTVSNSSLS EFAVLGFELG
YSMENPNSLV LWEAQFGDFS NGAQVIFDQF LSSGESKWLR QTGLVVCLPH GYDGQGPEHS
SARLERFLQM SDDNPYVIPE MDPTLRKQIQ QCNWQVVNVT TPANYFHVLR RQIHRDFRKP
LIVMSPKNLL RHKDCKSNLS EFDDLAGHPG FDKQGTRFKR LIKDQNNHKD LEEGINRLVL
CSGKVYYELD EERRKSERTD VAICRVEQLC PFPYDLIQRE LKRYPNAEIV WCQEEPMNMG
AYSYINPRLL TAMKVLGRGG IEDIKYVGRA PSAATATGFY SVHVQEQTEL VQKALQRDPL
NYPF
//