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Database: UniProt
Entry: A0A1J7H347_LUPAN
LinkDB: A0A1J7H347_LUPAN
Original site: A0A1J7H347_LUPAN 
ID   A0A1J7H347_LUPAN        Unreviewed;      1025 AA.
AC   A0A1J7H347;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=TanjilG_11922 {ECO:0000313|EMBL:OIW07288.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW07288.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW07288.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW07288.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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; CM007368; OIW07288.1; -; Genomic_DNA.
DR   RefSeq; XP_019452109.1; XM_019596564.1.
DR   RefSeq; XP_019452110.1; XM_019596565.1.
DR   RefSeq; XP_019452111.1; XM_019596566.1.
DR   AlphaFoldDB; A0A1J7H347; -.
DR   STRING; 3871.A0A1J7H347; -.
DR   EnsemblPlants; OIW07288; OIW07288; TanjilG_11922.
DR   GeneID; 109354219; -.
DR   Gramene; OIW07288; OIW07288; TanjilG_11922.
DR   KEGG; lang:109354219; -.
DR   OMA; CEDAFAH; -.
DR   OrthoDB; 3597773at2759; -.
DR   Proteomes; UP000188354; Chromosome LG08.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF32; OXOGLUTARATE DEHYDROGENASE (SUCCINYL-TRANSFERRING); 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:UP000188354};
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;  115839 MW;  F88C9B4F4DCCD794 CRC64;
     MAWFRAGASI AKHVIRRTLS QGGSSYLVSR ARALPPLSNG RKLHTTVFNK KAQAAPAPHP
     VPLSRLSDSF LDGTSSVYLE ELQRTWEADP SSVDESWDNF FRNFVGQSST TPGISGQTIQ
     ESMRLLLLVR AYQVNGHTKA KLDPLSLEER DVSEELDLGL YGFFEADLDR EFFLGVWRMA
     GFLSENRPVQ TLRSILTRLE QAYCGNIGYE YMHIADRNKC NWLRDKIETP TPIQFNRERR
     EVIFDRLTWS TLFENFLATK WTSAKRFGLE GGETLIPGMK EMFDRASDLG VESIVIGMAH
     RGRLNVLGNV VRKPLKQIFC EFSGGVQPED EVGLYTGTGD VKYHLGTSYD RPTRGGGRLH
     LSLVANPSHL EAVNPVVIGK TRAKQYYSND VGKLKNMGIL IHGDGSFAGQ GVVYETLHLS
     ALPNYSTGGT IHIVFNNQVA FTTDPSCGRS SQYCTDVAKA LDVPIFHVNG DDVEAVVHAC
     ELAAEWRQTF HSDVVVDLVC YRRFGHNEID EPSFTQPKMY KVIRSHPSAL EIYQKKLLET
     GELTKEDIDK IQKKVTSILN EEFMASKEYV PKRRDWLSAY WSGFKTPEQI SRIRNTGVKP
     EILKNVGKAI TTLPENFTPH RAVKRIYEQR AQMIETGEDI DWGCAEALAL ATLLVEGNHV
     RLSGQDVERG TFSHRHSVVH DQTTGEKYCP LDHVIMNQNE EMFTVSNSSL SEFGVLGFEL
     GYSMENPNSL VIWEAQFGDF ANGAHVIFDN FLVSGESKWL RQSGLVVLLP HGYDGQGPEH
     SSARLERFLQ MADDNPHVIP EMDSTLRKQI QECNLQIVNV TTPANFFHVL RRQIHREFRK
     PLIVMSPKNL LRSKACRSNL SEFDDVQGHP GFDKQGTRFK RLIKDQNDHS DREEGIRRLV
     LCSGKVYYEL DDQRTKVDAK DVAICRVEQL CPFPYDLVQR ELKRYPNAEI VWCQEEPLNM
     GGYPYVLPRL ISSLKAVGRG GYEDVKYVGR APSAATATGF LKVHQKEQAE IAEKALQRDP
     ISFPY
//
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