ID A4HPL4_LEIBR Unreviewed; 1012 AA.
AC A4HPL4;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 13-SEP-2023, entry version 88.
DE RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN ORFNames=LBRM_35_3700 {ECO:0000313|EMBL:CAM44122.1};
OS Leishmania braziliensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC Leishmania braziliensis species complex.
OX NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM44122.1, ECO:0000313|Proteomes:UP000007258};
RN [1] {ECO:0000313|EMBL:CAM44122.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44122.1,
RC ECO:0000313|Proteomes:UP000007258};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM44122.1, ECO:0000313|Proteomes:UP000007258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM44122.1,
RC ECO:0000313|Proteomes:UP000007258};
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; FR799010; CAM44122.1; -; Genomic_DNA.
DR RefSeq; XP_001568989.1; XM_001568939.2.
DR AlphaFoldDB; A4HPL4; -.
DR STRING; 5660.A4HPL4; -.
DR GeneID; 5419965; -.
DR KEGG; lbz:LBRM_35_3700; -.
DR VEuPathDB; TriTrypDB:LbrM.35.3700; -.
DR VEuPathDB; TriTrypDB:LBRM2903_350046800; -.
DR InParanoid; A4HPL4; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000007258; Chromosome 36.
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: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:CAM44122.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007258};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 660..868
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1012 AA; 114211 MW; 0923D4A3E9E86D67 CRC64;
MMRRLMSARG VLNCVSAVTP AIAFPRASQA TLIAGRHHAS DAMPERQLLY DNDSFLNGSS
AMYLEELYQQ WKKDPASVDA SWAELFSRSD LGSYDRALLD TPICVLPVES SDEGVVKQSL
ADCGRLTRMI QAFEDRGHLM AQTDPLNYME TDVTERTPSR RYKEMVRLDL AYFGFSDKDA
DRVVRVGFQN QMGGIYDTSS PPMMIRQLHE LLTAHYCGQI GFELVHLTDG EAKRFIRSQI
ELKDSSSALH RLISREEKLR IWDTVASAVF FEDFFKRKYS TQKRFGCDGA ETMVVGLRAL
LEKSCEFGIQ AINLGMAHRG RLNVLCHVIG KPFEVILKEF VGVTGQELLP FKIQSDVKYH
LGCRAQLKLH SGKVMETEML CNPSHLEAVN PFVQGYTRAM QVSLGEKGRE TVLPIEIHGD
AAFSGQGVAF ETMCISEVGE LHTGGTVHVV CNNQIGFTTD PKSSRSSAYC TDLGRVYNCP
ILHVNGDYPE EVVRVFEFAA EYRARFSKSV VIDLVCYRRF GHNENDDPSI TQPLMYERVR
AMPDVFQRYS DALIAQGVVT PQQVTQKAID EKARYGSYQD AAAHVNYAEY LKASIPAKWK
NMKYSDELGS VTQQPTAITH ETVNKVLKAL KTYPEGFQLH PKLKTVLDRR NATIETGEGI
EWGTAEALAF GSLLLEGHHV RVTGEDVERG TFAQRHAVVH DQSQVRSYIP LAHMSDMQGK
MIINNSPLSE YGMLGYAAGY SLYDPTSLVI WEAQYGDFAN GATIVFDQFL SAGESKWNQQ
QSCVVTLPHG YDGKGAEHSS GRLERFLQMS SEDVTTPAYS KEERAHRINW EITYPSTPAQ
YFHLLRRHQK RNFRKALIIF FSKQFLRAPN VSTLEELTSG EFQSVIPDPS VPGCQARRLV
MCTGQIYHYL NKYRETKGVK DVALVRVEEL SPFPVAEVQQ LLAEYEKAEL MWAQEEPRNM
GSWAHVEPRI EEYTNGEREL RYAGRCIAAA PSTGYKSKHD KEQEIICEMV FQ
//
