ID   TAL_PARP8               Reviewed;         317 AA.
AC   B2JE74;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Bphy_2104;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71282.1; -; Genomic_DNA.
DR   RefSeq; WP_012401488.1; NZ_CADFGH010000002.1.
DR   AlphaFoldDB; B2JE74; -.
DR   SMR; B2JE74; -.
DR   STRING; 391038.Bphy_2104; -.
DR   EnsemblBacteria; ACC71282; ACC71282; Bphy_2104.
DR   KEGG; bph:Bphy_2104; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_4; -.
DR   OMA; ICKFAED; -.
DR   OrthoDB; 784333at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001192; Chromosome 1.
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..317
FT                   /note="Transaldolase"
FT                   /id="PRO_1000126241"
FT   ACT_SITE        126
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   317 AA;  35090 MW;  64763C2294C31D9C CRC64;
     MTTALDQLKQ YTTVVADTGD FQQLAQYKPQ DATTNPSLVL KAVQKDEYKP LLEKTVRDHA
     SKPVGSIIDN LLIAFGTEIL KIVPGRVSTE VDARLSFDTK ASIDKAHELI KMYDAQGIGR
     ERVLIKLAST WEGIRAAEVL QKDGIKCNMT LLFSLAQAVA AAEAGAQLIS PFVGRIYDWY
     KKNAGSNWDE ARDGGANDPG VQSVRRIYAY YKKFGYPTEV MGASFRTTSQ ILELAGCDLL
     TISPDLLQKL HDSNDRIERK LSPEASRNAD IERVPTDEAS FRFLVNDDAM ATEKLSEGIR
     VFAADAIKLE KVIEALR