ID W7JVF6_PLAFO Unreviewed; 1038 AA.
AC W7JVF6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:KAF4330447.1};
DE SubName: Full=Oxoglutarate dehydrogenase (Succinyl-transferring), E1 component {ECO:0000313|EMBL:EWC88998.1};
GN ORFNames=CK202_2392 {ECO:0000313|EMBL:PKC47505.1}, CYL21_1532
GN {ECO:0000313|EMBL:KAF4330447.1}, PFNF54_02268
GN {ECO:0000313|EMBL:EWC88998.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC88998.1, ECO:0000313|Proteomes:UP000030673};
RN [1] {ECO:0000313|EMBL:EWC88998.1, ECO:0000313|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:EWC88998.1,
RC ECO:0000313|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKC47505.1, ECO:0000313|Proteomes:UP000232684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:PKC47505.1};
RA Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT "Plasmodium falciparum NF54 genome assembly.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4330447.1, ECO:0000313|Proteomes:UP000754359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:KAF4330447.1};
RA Baumgarten S., Treeck M., Scherf A.;
RT "Genome assembly of Plasmodium falciparum NF54 DiCre.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; KE123791; EWC88998.1; -; Genomic_DNA.
DR EMBL; QFXU01000009; KAF4330447.1; -; Genomic_DNA.
DR EMBL; NYMT01000006; PKC47505.1; -; Genomic_DNA.
DR AlphaFoldDB; W7JVF6; -.
DR SMR; W7JVF6; -.
DR EnsemblProtists; EWC88998; EWC88998; PFNF54_02268.
DR VEuPathDB; PlasmoDB:PfNF54_080024500; -.
DR OMA; IRIRRHN; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR Proteomes; UP000754359; Unassembled WGS sequence.
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:UP000030673};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 650..860
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 1038 AA; 121150 MW; 8359B70B2C2F2A36 CRC64;
MRKFFYTNNL VRNNGKDIRT RSFHLSSCLY DYNFNPSMTS YIENTYKIWK EDRNNLHKSW
DSLFSMYPHA EMDNYNNPIK INRKTDNYNN SNCFQDVLKN NNLRITYVNN EMLEKGKTEN
IYDLARIVQL IRWYQKKGHL YANINPLPLP KEPPYSSVCY EPCKRKMSYV DFGFNEDDLD
KEFFFDLPSI SGFSSNGMKK CNLRNLLKRL EETYCGTIGF EYMHITNENI VNYIIQRIEK
DKKYEYDTKM KKRILEYTAR AFIFENYMAA KFATTKRFGV DGCETLITGM KALIKRAAQL
DVDSVLMSMS HRGRLNVLFN VLHKPLEQMM SEFRGKTGFS DNIWGNTGDV KYHLGVEIDY
YDEDSQRYIH MGIVDNSSHL ESVDPILMGQ ARAQQYYCND KEKKKVLPIT IHGDASIAGQ
GIAYETFQMS KLPSYNVGGT IHIVVNNQIG FTTYPIDARS GKYCTDIAKC IDIPIIHVNA
DDPEAVTYVF ELALDIRNKF NIDTIIDIVG YRRFGHNELD MPKFTNPLLY DVIARHKSVL
DIYSKKLIDE NIISLKEFED NKTEIFNFYE QVYEKSKSFV PTPKEKYLPQ WEHMVTPQKF
SPSRKTGVEK DVLINLGKKI FTLRENFTAH PIITKLFKSR IDSLETGKNI DFGTAELLAY
ATLLSDGFHA RLSGQDSQRG TFSHRHAVLH DQITYESYNI FDSLKTPHTI EVNNSLLSEY
ACLGYEIGYS YEHPDALVIW EAQFGDFANG AQVMIDNYIA SGETKWNKQS GIVMLLPHGY
DGQGPEHSSA RIERFLQLCD DREDIATYSV EKDNKIIQQH NMQVINCSKP SNFFHALRRQ
MHRSFRKPLI VITPKKMLKM RMAFDKIENF LTNTEFLPYL PEEVGHKLKD KKEIKRIILC
SGQVYYDLLN YRYTNKIDDV AIARIEQLSP FPFKQIMNDL QTYPNLRDII WAQEEHMNMG
PWFYVSRRIE ASIKQLKKDK PKWNIQIPQV RYSGRDVYAA QSAGDLNLHL YQLDEFLVDA
FNLDKKYNMH VQKYTDAL
//
