ID   A4HFL1_LEIBR            Unreviewed;      1007 AA.
AC   A4HFL1;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Putative 2-oxoglutarate dehydrogenase subunit {ECO:0000313|EMBL:CAM45373.1};
GN   ORFNames=LBRM_27_0960 {ECO:0000313|EMBL:CAM45373.1};
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:CAM45373.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM45373.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM45373.1,
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:CAM45373.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM45373.1,
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; FR799002; CAM45373.1; -; Genomic_DNA.
DR   RefSeq; XP_001565855.1; XM_001565805.1.
DR   AlphaFoldDB; A4HFL1; -.
DR   STRING; 5660.A4HFL1; -.
DR   GeneID; 5416716; -.
DR   KEGG; lbz:LBRM_27_0960; -.
DR   VEuPathDB; TriTrypDB:LbrM.27.0960; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_270015500; -.
DR   InParanoid; A4HFL1; -.
DR   OMA; IRIRRHN; -.
DR   Proteomes; UP000007258; Chromosome 27.
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; 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; 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:UP000007258};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          631..847
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1007 AA;  113532 MW;  F3C0A9DF3CC6953D CRC64;
     MMRRALSGVI AVRASAMRNY TDARTIRQPN PYDQLVNAEN QHYVENLMRQ YEADSALVDP
     SWVPVLEAIR SRNDDAPVVS TFSRPIDAKS LSEKQRHDNM RLSWMIREYE RFGHHMAKVN
     PLSGYHADNR ILGSRTLAPE EFCFSKEDLK LVFNVTLGAS YDATFVSGGT SMTLQEIIDQ
     LRRFYCGPIG FEFMSSGFFE LRNWFRHEVA NSLQPLPDEE RKLYYKDVIK ACGFEKFLQV
     KYATKQRFGL DGGEALIPAL NAVILTSSNL GVQSAIIGMA HRGRLNVLAN VLHKSLRTIL
     NEFEGRVAIE NVHVSGDVEY HLGKRKHVKL ANNKLIELDL LPNPSHLEAV NPLVLGKAHA
     RQVYTDDVEC TTVLPILIHG DAAFAGQGSC YETMGFCELE NFHVGGTLHL VINNQIGFTT
     NPKDSRASAY CTDLSKVNNA PVMHVNGDDV DACVKAAKIA ARFRHQFHRD IIIDLVCYRR
     NGHNETDMPD FTQPQLYEQI RRHPCLVDIY TKTLIEDGTL TAEEAKVEKT EWDSVLRQAY
     ERMNSTQNFV KVMPVFDPES ENTSADLSYA KIAAARVPRP APAVETGVEA QTLRAAGVHL
     ASIPKEMQKP HPVVERTYAA RKKGTEQGDA IEWCQAELMA LATLSMQGVP IRLTGEDVER
     GTFTQRHAGI TDMKTNLKYF PVKTVSPSQA LITISNSSLS ELGVCGFEMG YNMENTRSIT
     MWEAQFGDFA NGAQVIFDQF LSCCEEKWNE HSNLILSLPH GYSGAGPEHS SARVERFLQL
     SDDSDRVPSD FRHFSNDQAL EIRIRRHNWQ VTYPSTPANY FHLLRRQGLR EFPKPLVNFF
     SKARLRAPNL SKLADMAQGS RFKAVIDTAR TEDTVARKVA FCSGQIESIV NDAKTAMQKE
     TPGVHDDIVL VTVEQLAPFP WEQVADVMEK YAQRNPDTEF VWLQEEPRNM GMWMHMRPRM
     NSLMRHLGLK QNRINVVSRS SSASPSTGYG SVHVEEEKKL IQEIIAG
//