ID A0A1U7YGN8_NICSY Unreviewed; 1020 AA.
AC A0A1U7YGN8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=LOC104244628 {ECO:0000313|RefSeq:XP_009798399.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009798399.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009798399.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009798399.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_009798399.1; XM_009800097.1.
DR AlphaFoldDB; A0A1U7YGN8; -.
DR SMR; A0A1U7YGN8; -.
DR STRING; 4096.A0A1U7YGN8; -.
DR GeneID; 104244628; -.
DR KEGG; nsy:104244628; -.
DR eggNOG; KOG0450; Eukaryota.
DR OrthoDB; 3597773at2759; -.
DR Proteomes; UP000189701; Unplaced.
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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 635..848
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1020 AA; 115583 MW; 19C792274A83BCB3 CRC64;
MAWFRAGSSV AKLAIRRAVS QGGSYVPRSR LLPSQSRYFH TTVIRPKAQS APVPRPVPLS
KLTDSFLDGT SSVYLEELQR TWEQDPNSVD ESWDNFFRNF VGLAATSPGI SGQTIQESMN
LLLLVRAYQV NGHMKAKLDP LALEEREIPD VLDPVSYGFT EADLDREFFL GVWRMSGFLS
ENRPVQTLRA ILTRLEQAYC GSIGFEYMHI PDRDKCNWLR ERIETPTPRE YNRERREVIL
DRLMWSTQFE NFLATKWMAA KRFGLEGCET LIPGMKEMFD RSADLGVESI VIGMPHRGRL
NVLGNVVRKP LRQIFSEFSG GTKPADGAGY VGTGDVKYHL GTSYDRPTRG GKRIHLSLVA
NPSHLEAVDP VVVGKTRAKQ YYSNDVDRTK NMGVLLHGDG SFAGQGVVYE TLHLSALPNY
TTGGTIHIVV NNQVAFTTDP RSGRSSQYCT DVAKALSAPI FHVNGDDVEG VVHACELAAE
WRQTFHSDVV VDIVCYRRFG HNEIDEPSFT QPKMYKVIRS HPSALEIYQN KLLQSGQVTK
DDVEKIHNKI NTILNEEFVA SKDYIPQKRD WLSAFWSGFK SPAQLSRVRN TGVKPEILKD
VGKAITTLPE DFKPHRAIKK VYDERKKMIE TGERVDWALG EALAFATLLV EGNHVRLSGQ
DVERGTFSHR HSVLHDQETG AKYCPLDHVM MNQNEEMFTV SNSSLSEFGV LGFELGYSME
NPNSLVLWEA QFGDFSNGAQ VIFDQFLSSG EAKWLRQTGL VVLLPHGYDG QGPEHSSARL
ERFLQMSDDN PFVIPEMEPT LRKQIQECNW QVVNVTTPAN YFHVLRRQIH RDFRKPLIVM
SPKNLLRHKE CKSNLSEFDD VQGHPGFDKQ GTRFKRLIKD QNDHSDLEEG IRRLVLCSGK
VYYELDEERK KVDGKDVAIC RVEQLSPFPY DLVQRELKRY PNAEIVWCQE EPMNMGAYSY
IAPRLCTAMK ALGRGDMDDI KYVGRAPSAA TATGFQQVHV KEQTELVQKA LQQDPINSPF
//
