ID   TAL_CUPMC               Reviewed;         318 AA.
AC   Q1LLK8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Rmet_2089;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08968.1; -; Genomic_DNA.
DR   RefSeq; WP_011516802.1; NC_007973.1.
DR   AlphaFoldDB; Q1LLK8; -.
DR   SMR; Q1LLK8; -.
DR   STRING; 266264.Rmet_2089; -.
DR   EnsemblBacteria; ABF08968; ABF08968; Rmet_2089.
DR   KEGG; rme:Rmet_2089; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_4; -.
DR   OMA; KFGYKTL; -.
DR   OrthoDB; 784333at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002429; 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.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..318
FT                   /note="Transaldolase"
FT                   /id="PRO_1000014517"
FT   ACT_SITE        126
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   318 AA;  34919 MW;  22FB34901FE6586B CRC64;
     MNELEQLRQF TTVVADTGDF QLMKQYKPQD ATTNPSLIFK AVQKPEYRPL LEQAVRDHHG
     NSGLDGVMDQ LLIAFGCEIL AIVPGRVSTE VDARLSFDTE ATVAKARHLI GLYEQRGVAR
     ERVLIKIAST WEGIRAAEVL QRENIRCNMT LLFSLAQAVA CAEAGAQLIS PFVGRILDWY
     KKQAGEKWDP VANGGENDPG VRSVRQIYDY YKKFGYATEV MGASFRGTDQ ILSLAGCDLL
     TISPELLEQL AGGQSAVALK LSVEQAQAGN VARIAADEPA FRWQLNEDAM ATEKLSEGIR
     LFAADAVKLE KLVGELAS