ID Q4Q171_LEIMA Unreviewed; 979 AA.
AC Q4Q171;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=LMJF_36_3470 {ECO:0000313|EMBL:CAJ09310.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ09310.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ09310.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ09310.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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; FR796432; CAJ09310.1; -; Genomic_DNA.
DR RefSeq; XP_001686927.1; XM_001686875.1.
DR AlphaFoldDB; Q4Q171; -.
DR STRING; 5664.Q4Q171; -.
DR EnsemblProtists; CAJ09310; CAJ09310; LMJF_36_3470.
DR GeneID; 5655638; -.
DR KEGG; lma:LMJF_36_3470; -.
DR VEuPathDB; TriTrypDB:LmjF.36.3470; -.
DR VEuPathDB; TriTrypDB:LMJFC_360048700; -.
DR VEuPathDB; TriTrypDB:LMJLV39_360044900; -.
DR VEuPathDB; TriTrypDB:LMJSD75_360044800; -.
DR eggNOG; KOG0450; Eukaryota.
DR HOGENOM; CLU_004709_1_0_1; -.
DR InParanoid; Q4Q171; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000000542; Chromosome 36.
DR GO; GO:0036064; C:ciliary basal body; ISO:GeneDB.
DR GO; GO:0097014; C:ciliary plasm; ISO:GeneDB.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
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; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23152:SF12; 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 ECO:0000313|EMBL:CAJ09310.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 627..835
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 979 AA; 111106 MW; A28F352A248AA885 CRC64;
MGRRRAAEAV PERQLLFDND SFLSGSSAMY MDGLYQQWKK DPASVDASWA ELFSRSDLGN
YNHALLDTPI CVLPAKSSDE AVVKQSLADC GRLIRMIHTF EDRGHLMAQT DPLNYVDTDV
TERTPSRRYK EMVRLDLAYF GFSDKDLDRV VRVGFQNQMG GIYDTSSPQL TIRQLHELLT
ERYCGRIGFE LVHLTDGDAK RFVRSQIELK DGCSALHRPM SREERLRIWD TVASAVFFED
FFKRKYSTQK RFGCDGAESM VAGLRALLEK SSELGVQAIN LGMAHRGRLN VLCHVIGKPF
EVILKEFVGV TGQELHPFQI QSDVKYHLGY RGQLKLNSGK VMETEMLFNP SHLEAVNPFV
QGYTRAMQVS LGEKGREKVL PIEIHGDAAF AGQGVAFETM CISEVGEQDT GGTVHVVCNN
QIGFTTDPKS SRSSAYCSDL GRVYNCPILH VNGDYPEEVI RVFEFAAEYR ARFHKSVVID
LVCYRRFGHN ENDDPSITQP LMYERVRAMP DVFRRYTDAL ITQGILTPQQ STQKAIDEKA
RYGSYQEAAA QVNYAEYLKK SIPDKWKCMK YSDELGNVTQ HPTAITQETV DKVLKALKTY
PEGFQLHPKL KAVLDRRNET IETGEGIEWG TAEALAFGSL LLEGHQVRVT GEDVERGTFA
QRHAVIHDQS QERTYVPLAH ISDTQGRMII NNSPLSEYGM LGYAAGYSLY DPTSLVIWEA
QYGDFANGAT IVFDQFLSAG ESKWNQQQSC IVTLPHGYDG KGAEHSSGRL ERFLQMSSED
VTTPAYSKEE RAHRINWEIT YPSTPAQYFH LLRRHQKRNF RKALVIFFSK KYLRAPNVST
LEELTSGEFQ PVIPDLSVPA SQARRLVMCT GQIYHYLNKY RETKGVKDVA LVRVEELSPF
PVAEVQQLLA EYEKAELMWA QEEPKNMGSW AHVEPRIEDY TKGERELRYA GRSITAAPST
GYKSKHEKEQ EIICEMVFH
//
