ID TAL_BORPA Reviewed; 320 AA. AC Q7WAY2; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 04-NOV-2026, entry version 114. 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=BPP1228; OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Alcaligenaceae; Bordetella. OX NCBI_TaxID=257311; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX640426; CAE36530.1; -; Genomic_DNA. DR RefSeq; WP_010926156.1; NC_002928.3. DR AlphaFoldDB; Q7WAY2; -. DR SMR; Q7WAY2; -. DR GeneID; 93202985; -. DR KEGG; bpa:BPP1228; -. DR HOGENOM; CLU_047470_0_1_4; -. DR OMA; AACNDKV; -. DR UniPathway; UPA00115; UER00414. 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:000131; 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; 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; Schiff base; Transferase. FT CHAIN 1..320 FT /note="Transaldolase" FT /id="PRO_0000173580" 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 320 AA; 34813 MW; BE6C6C6D54F84F06 CRC64; MPSQLEALRR HTVVVADTGD FEAMRALRPT DATTNPSLIL KAVQQEAYRP LLVQTARAHQ GASPAEITDR LLVAFGRQIL DIVPGRVSTE VDARLSFDTR ATVERARGLI ALYQAAGVPR ERVLIKIAST WEGIQAARVL QAEGIRCNLT LLFCLPQAAA CADAGVQLIS PFVGRIYDWH KKNAGAEWVE DARRGANDPG VQSVSRIYRY YKRFGIETEI MGASFRNVDQ ILALAGCDLL TISPELLTRL SQTEGEVPAA LSPQAGHDDA DAVRLDGGEV AFRTQLNEDA MASEKLSEGI RLFVADARKL DALIESHGAA //