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Entry: X6PBN2_RETFI
LinkDB: X6PBN2_RETFI
Original site: X6PBN2_RETFI 
ID   X6PBN2_RETFI            Unreviewed;       464 AA.
AC   X6PBN2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
DE   Flags: Fragment;
GN   ORFNames=RFI_01601 {ECO:0000313|EMBL:ETO35464.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO35464.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO35464.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
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   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETO35464.1}.
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DR   EMBL; ASPP01001573; ETO35464.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6PBN2; -.
DR   EnsemblProtists; ETO35464; ETO35464; RFI_01601.
DR   OMA; EYRWTSG; -.
DR   OrthoDB; 5399939at2759; -.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 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; IPR020826; Transketolase_BS.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          100..274
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETO35464.1"
SQ   SEQUENCE   464 AA;  51778 MW;  963F6EA7C2293B54 CRC64;
     EDTHGVHGSP LGPEVLADFK RKNGFDPKES FVVSEKVRQK YEETILSRGQ QAEKAWNDLL
     EKYSREYKDE GLVLKRILSG ELPKDWQKGL PTFNAQTPSD ATRNINGKIL NNIADVLPEL
     IGGCADLTPS TKTDIKKSHD FQSNSYDGRY FRFGVREFGM FAICNGIAAY GSGLIPFSST
     FLNFITYGWG AVRLGALSHL RQIYIMTHDS VFLGEDGPTH QPIEVLPLMR ATPNLYTFRP
     ADGNEIVGSW IVAVEKLRHS GIVLCLSRQN VVSLDNTSRE GVSHGIYHLA TFDKESKETE
     HPVVLISTGS EVGPTFGAAK LLNSKHHLTV HVLSAPCLEL FAQQPLEYKK KLLGKGLVIS
     VEAASTSSWQ KYSHYQIGVD RYGASANLKD IAKFFGFTDE LIADKVLQYR ELVKDITLPL
     LPCLLPSLKL YIIEILFLGV GIKRKTTQKF TLILLCCFII KRIL
//
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