ID W4IM73_PLAFA Unreviewed; 672 AA.
AC W4IM73;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=PFNF135_01456 {ECO:0000313|EMBL:ETW44205.1};
OS Plasmodium falciparum NF135/5.C10.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1036726 {ECO:0000313|EMBL:ETW44205.1, ECO:0000313|Proteomes:UP000019114};
RN [1] {ECO:0000313|EMBL:ETW44205.1, ECO:0000313|Proteomes:UP000019114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF135/5.C10 {ECO:0000313|EMBL:ETW44205.1,
RC ECO:0000313|Proteomes:UP000019114};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum NF135/5.C10.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW44205.1, ECO:0000313|Proteomes:UP000019114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF135/5.C10 {ECO:0000313|EMBL:ETW44205.1,
RC ECO:0000313|Proteomes:UP000019114};
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 NF135/5.C10.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; KI926031; ETW44205.1; -; Genomic_DNA.
DR AlphaFoldDB; W4IM73; -.
DR EnsemblProtists; ETW44205; ETW44205; PFNF135_01456.
DR Proteomes; UP000019114; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 358..529
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 672 AA; 75829 MW; C8BDDBF3510CE872 CRC64;
MNIMDKEIDT KCINEIRMLS AELPLEAKSG HQGAPIGCAP IAHILWSYVM NYYNEDTKWI
NRDRFILSNG HASALLYTML YLTEQGLSME DLKSFRQFGS LTPGHPENHI TKGVEVTTGP
LGQGASNAVG MAIAAHNLAD KYNTEEHKIF DNYVYAICGD GCMQEGVFCE AASLAGHLGL
GRLILLYDDN KITIDGNTDL SFTENIEKKF EALNWEVRRV EDGNKDYKKI LHEIEQGKKN
LQQPTLIIVR TACGFGTKVE GTCKSHGLAL NDEDLKNAKS FFGLDPQKKF HISDEVKEFY
KNVIQKKKEN YIKWKNMFDD FSLKYPQVSQ EIIRRFQNDL PNNWKDALPK YTPKDAPGAT
RNLSGIVLNS INKIFPELIG GSADLSESNC TSLKEENDIK KNSYGNKYIR FGVREHGMVA
ITNGLYAYGG FKPYCGTFLN FYTYAFGALR LAALSNHHIL CIATHDSVEL GEDGPTHQPI
EVLSLLRSTP NLNIIRPADG NEVSGAYLSH FSNPHTPTVI ALCRNKVPHL NNTQPEQVLK
GAYILEDFDT SNNPKVILTG SGSELHLCFE AKEILKNQHQ LNVRIVSFPS WTLFKKQPED
YQYSVMMHNH PNLPRFYIEP ASTHGFDTYF NVYIGINQFG YSAPKNKIWE HLGFTPENIV
QKVLAFMKNK LK
//
