ID   C0PHB0_MAIZE            Unreviewed;      1025 AA.
AC   C0PHB0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=100383579 {ECO:0000313|EnsemblPlants:Zm00001eb085340_P001};
GN   ORFNames=ZEAMMB73_Zm00001d003947 {ECO:0000313|EMBL:ONM18037.1};
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:ACN34576.1};
RN   [1] {ECO:0000313|EMBL:ACN34576.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACN34576.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EMBL:ONM18037.1, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb085340_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM18037.1};
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.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb085340_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb085340_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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; BT067679; ACN34576.1; -; mRNA.
DR   EMBL; CM007648; ONM18037.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18038.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18040.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18041.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18042.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18046.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18049.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18050.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18051.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18052.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18058.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18066.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM18069.1; -; Genomic_DNA.
DR   RefSeq; NP_001169698.1; NM_001176227.1.
DR   RefSeq; XP_008668443.1; XM_008670221.1.
DR   RefSeq; XP_008668444.1; XM_008670222.1.
DR   AlphaFoldDB; C0PHB0; -.
DR   PaxDb; 4577-GRMZM2G142863_P01; -.
DR   EnsemblPlants; Zm00001eb085340_T001; Zm00001eb085340_P001; Zm00001eb085340.
DR   EnsemblPlants; Zm00001eb085340_T002; Zm00001eb085340_P002; Zm00001eb085340.
DR   GeneID; 100383579; -.
DR   Gramene; Zm00001eb085340_T001; Zm00001eb085340_P001; Zm00001eb085340.
DR   Gramene; Zm00001eb085340_T002; Zm00001eb085340_P002; Zm00001eb085340.
DR   KEGG; zma:100383579; -.
DR   eggNOG; KOG0450; Eukaryota.
DR   HOGENOM; CLU_004709_1_0_1; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; C0PHB0; 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; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   1: Evidence at protein level;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:C0PHB0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          640..853
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1025 AA;  116203 MW;  3D261A248CF01992 CRC64;
     MGLFRAASGL ARLALRRNLS RAAASPFAGS GGAVPGAMPA RYFHSTRPRR FAAPAPRAVP
     LSRLTDSFLD GTSSVYLEEL QRAWEADPNS VDESWDNFFR NFVGQAAATS PGLSGQTIQE
     SMRLLLLVRA YQVSGHLKAK LDPLGLEERP VPDVLDPGFY GFSEADLDRE FFLGVWMMAG
     FLSENRPVQT LRSVLERLEQ AYCGTIGYEY MHIPDREKCN WLRDRIETVN PREYTYDRRQ
     VMLDRLIWST QFENFLATKW TTAKRFGLEG AETLIPGMKE MFDRAADLGV ESIVIGMPHR
     GRLNVLGNVV RKPLRQIFSE FSGGTKPVNE GEGLYTGTGD VKYHLGTSYD RPTRGGKHIH
     LSLVANPSHL EAVDPVVAGK TRAKQYYSND RDRTKNLGVL LHGDGSFSGQ GVVYETLHLS
     ALENYTTGGT IHIVVNNQVA FTTDPRSGRS SQYCTDVAKA LDAPIFHVNG DDLEAVVHVC
     ELAAEWRQTF HSDVVVDIVC YRRFGHNEID EPSFTQPKMY KVIRNHPSAL EIYQRKLLES
     GKISKEDIDK LNKKVSTILN EEFQNSKDYV PNKRDWLSAY WTGFKSPEQI SRIQNTGVKP
     EILKRVGEAM TTLPENFNPH RAVKKIFYQR RQMIETGEGI DWAVGEALAF ATLIIEGNHV
     RLSGQDVERG TFSHRHSVLH DQETGEQYCP LDHLVMNQDE ELFTVSNSSL SEFAVLGFEL
     GYSMENPNSL VIWEAQFGDF SNGAQVIFDQ FLSSGESKWL RQTGLVVCLP HGYDGQGPEH
     SSARLERFLQ MSDDNPYVIP EMDPTLRKQI QQCNWQVVNV TTPANYFHVL RRQIHRDFRK
     PLIVMSPKNL LRHKDCKSNL SEFDDLAGHP GFDKQGTRFK RLIKDQNNHK DLEEGINRLV
     LCSGKVYYEL DEERRKTERT DVAICRVEQL CPFPYDLIQR ELKRYPNAEI VWCQEEPMNM
     GAYSYINPRL LTAMKALGRG GIEDIKYVGR APSAATATGF YSVHVQEQTE LVQKALQRDP
     INYPF
//