ID   TAL_BURM1               Reviewed;         317 AA.
AC   A9AIJ8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   04-NOV-2026, entry version 104.
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};
GN   OrderedLocusNames=Bmul_0942, BMULJ_02322;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia;
OC   Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase involved in the non-oxidative phase in the
CC       pentose phosphate pathway. Catalyzes the reversible conversion of
CC       sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is
CC       important for the balance of metabolites in the pentose-phosphate
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate =
CC         D-erythrose 4-phosphate + beta-D-fructose 6-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:0000255|HAMAP-Rule:MF_00492}.
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; CP000868; ABX14633.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44217.1; -; Genomic_DNA.
DR   RefSeq; WP_006413476.1; NC_010084.1.
DR   AlphaFoldDB; A9AIJ8; -.
DR   SMR; A9AIJ8; -.
DR   STRING; 395019.BMULJ_02322; -.
DR   KEGG; bmj:BMULJ_02322; -.
DR   KEGG; bmu:Bmul_0942; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_4; -.
DR   OMA; AACKMPE; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008815; 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   FunFam; 3.20.20.70:FF:000002; Transaldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; NF009001; PRK12346.1; 1.
DR   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 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_1000126240"
FT   ACT_SITE        90
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   ACT_SITE        126
FT                   /note="Nucleophile; Schiff-base intermediate with
FT                   substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         17
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         35
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         126
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         148
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         170
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         175
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         224
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   BINDING         226
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   317 AA;  35380 MW;  19AF5564EEBFDB29 CRC64;
     MTTALDQLKQ YTTVVADTGD FQQLAQYQPQ DATTNPSLIL KAVQKDAYKP ILEKTVRDHR
     NESTDFIIDR LLIAFGTEIL KIIPGRVSTE VDARLSFDAK RSIDKAHELI KLYEAAGIER
     DRILIKLAST WEGIRAAETL QKEGIKCNMT LLFSLVQAAA CAEAGAQLIS PFVGRIYDWY
     KKQAGADWDE AKNGGANDPG VQSVRRIYTY YKTFGYKTEV MGASFRTTSQ IVELAGCDLL
     TISPDLLQKL HDSNETVTRK LSPDALHDKP TERVAIDEAS FRFQLNDEAM ATEKLAEGIR
     VFAADAVKLE KLIEALR
//