ID A0A061FU17_THECC Unreviewed; 1023 AA.
AC A0A061FU17;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=TCM_042828 {ECO:0000313|EMBL:EOY18229.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY18229.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY18229.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001888; EOY18229.1; -; Genomic_DNA.
DR EMBL; CM001888; EOY18230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FU17; -.
DR STRING; 3641.A0A061FU17; -.
DR EnsemblPlants; EOY18229; EOY18229; TCM_042828.
DR EnsemblPlants; EOY18230; EOY18230; TCM_042828.
DR Gramene; EOY18229; EOY18229; TCM_042828.
DR Gramene; EOY18230; EOY18230; TCM_042828.
DR eggNOG; KOG0450; Eukaryota.
DR InParanoid; A0A061FU17; -.
DR OMA; IRIRRHN; -.
DR Proteomes; UP000026915; Chromosome 10.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 636..849
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1023 AA; 115829 MW; 62131CB72B7F833C CRC64;
MGWFRAGSSV AKLASRRTLS QGGLYTARSR IVPSQNHYFH TTVFKSKAQS APVPRPVPLS
KLTDSFLDGT SSVYLEELQR AWEADPDSVD ESWDNFFRNF VGQAATSPGI SGQTIQESMR
LLLLVRAYQV NGHMKAKLDP LGLEEREIPD DLDPALYGFT EADLDREFFL GVWRMSGFLS
ENRPVQTLRS ILTRLEQAYC GSIGFEYMNI ADREKCNWLR DKIETPTPMQ YNRQRREVIL
DRLIWSTQFE NFLATKWTTA KRFGLEGGET LIPGMKEMFD RAADLGVESI VIGMPHRGRL
NVLGNVVRKP LRQIFSEFSG GTKPVDEVGL YTGTGDVKYH LGTSYDRPTR GGKRIHLSLV
ANPSHLEAVD PVVVGKTRAK QYYSNDVDRT KNMAVLIHGD GSFAGQGVVY ETLHLSALAN
YTTGGTIHIV VNNQVAFTTD PRAGRSSQYC TDVAKALNAP IFHVNGDDVE AVVHACELAA
EWRQTFHSDV VVDLVCYRRF GHNEIDEPSF TQPKMYKIIR NHPSALQIYQ NKLLESGQVM
KEDIGWISEK VSKILNEEFL ASKDYVPKRR DWLSAYWTGF KSPEQLSRVR NTGVKPEILK
NVGKAITTLP DNFKPHRAVK KVYDQRAQMI ETGEGLDWAI GEALAFATLL VEGNHVRLSG
QDVERGTFSH RHSVLHDQET GEQYCPLDHV IINQNEEMFT VSNSSLSEFG VLGFELGYSM
ENPNSLVMWE AQFGDFANGA QVIFDQFLSS GESKWLRQTG LVVLLPHGYD GQGPEHSSAR
LERYLLMSGD NPFVIPEMDP TLRTQIQECN WQVVNVTTPA NYFHVLRRQI HREFRKPLIV
MSPKNLLRHK DCKSNLSEFD DVQGHPGFDK QGTRFKRLIK DQNMHSDLEE GIRRLVLCSG
KVYYELDDER KKNKATDVAI CRVEQLCPFP YDLIQRELKR YPNAEIVWCQ EEPMNMGAFS
YIAPRLATSM QALGRGTFED IKYVGRAPSA STATGFYVVH VKEQTELVQK AIQPEPIKFH
APV
//
