ID Q8FT75_COREF Unreviewed; 360 AA. AC Q8FT75; C8NP05; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 02-SEP-2026, entry version 137. DE RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|NCBIfam:TIGR00876}; DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|NCBIfam:TIGR00876}; GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493}; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18505.1, ECO:0000313|Proteomes:UP000001409}; RN [1] {ECO:0000313|EMBL:BAC18505.1, ECO:0000313|Proteomes:UP000001409} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395 RC {ECO:0000313|Proteomes:UP000001409}; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(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:0000256|HAMAP-Rule:MF_00493}. 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:0000256|HAMAP-Rule:MF_00493}; 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:0000256|HAMAP-Rule:MF_00493}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily. CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}. 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; BA000035; BAC18505.1; -; Genomic_DNA. DR RefSeq; WP_006767696.1; NC_004369.1. DR AlphaFoldDB; Q8FT75; -. DR STRING; 196164.gene:10742116; -. DR KEGG; cef:CE1695; -. DR eggNOG; COG0176; Bacteria. DR HOGENOM; CLU_050771_1_0_11; -. DR OrthoDB; 9809101at2; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule. DR CDD; cd00955; Transaldolase_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00493; Transaldolase_2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR004732; Transaldolase_2. DR InterPro; IPR018225; Transaldolase_AS. DR NCBIfam; NF002881; PRK03343.1; 1. DR NCBIfam; TIGR00876; tal_mycobact; 1. DR PANTHER; PTHR10683; TRANSALDOLASE; 1. DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1. DR Pfam; PF00923; TAL_FSA; 1. DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00493}; KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP- KW Rule:MF_00493}; Reference proteome {ECO:0000313|Proteomes:UP000001409}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP- KW Rule:MF_00493}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00493}. FT ACT_SITE 108 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT ACT_SITE 139 FT /note="Nucleophile; Schiff-base intermediate with FT substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 17 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 44 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 139 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 161 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 200 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" FT BINDING 205 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493" SQ SEQUENCE 360 AA; 39110 MW; 661CCDFE38259434 CRC64; MSHIDDLSQL GTSTWLDDLS RDRISTGNLK QVIEEKSIVG VTTNPAIFAA AMSKGNAYDD QIDQLKTAGA SVDEAVYAMS IDDVRDACDL FTDIYESTGG YDGRVSIEVD PRISADAAAT LEQAKELWAK VDRPNVMIKI PATPGSLPAI SDALAEGISV NVTLIFSVDR YRQVIKAYID GVKRAAENGH DVSKIHSVAS FFVSRVDTEI DRRLEEIGTD EALELRGKAG VANARRAYAL YRELFAEADL PEGANTQRPL WASTGVKNPD YPATLYVSEL AGPDTVNTMP EGTIDAVLEQ GNLHGDTLTD TADEAEQLFT RLGELGVDLG DVFEVLENEG VEKFVASWSE LLESMEARLK //