ID   TAL_RALSO               Reviewed;         319 AA.
AC   Q8Y014;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=RSc1231;
GN   ORFNames=RS02738;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00492};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC       step 2/3. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR   EMBL; AL646052; CAD14933.1; -; Genomic_DNA.
DR   RefSeq; WP_011001180.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y014; -.
DR   SMR; Q8Y014; -.
DR   STRING; 267608.RSc1231; -.
DR   EnsemblBacteria; CAD14933; CAD14933; RSc1231.
DR   GeneID; 60500752; -.
DR   KEGG; rso:RSc1231; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_4; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001436; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..319
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173610"
FT   ACT_SITE        125
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   319 AA;  34844 MW;  122EA771D47082AC CRC64;
     MTQLDQLKQF TTVVADTGDF QAMRAYAPHD ATTNPSLILK AVQKAEYRPL LEQAVRDARS
     DSVEDIIDAV LVAFGCEILS IIPGRVSTEV DARLSFDTAA TVAKARHLIA LYEARGVPRE
     RVLIKIASTW EGIRAADQLR AEGIRCNMTL LFSLIQAVAC AEAGVQLISP FVGRIYDWYK
     KDAGAAWDPI AQGGANDPGV QSVVRIYNYY KRFGYTTEVM GASFRNTSQI IELAGCDLLT
     ISPELLAQLQ QSDAPVERKL SPEHAHATNL VRLPADEAAF RWHMNADAMA TEKLAEGIRL
     FAADAVKLEG LIGPLRAAA