ID TAL2_NOSP7 Reviewed; 381 AA. AC P48983; B2J6J8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 10-JUN-2026, entry version 124. DE RecName: Full=Transaldolase 2; DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493}; GN Name=tal2; OrderedLocusNames=Npun_F4024; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Nostoc. OX NCBI_TaxID=63737; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7870816; DOI=10.1104/pp.107.1.267; RA Summers M.L., Meeks J.C., Chu S., Wolf R.E. Jr.; RT "Nucleotide sequence of an operon in Nostoc sp. strain ATCC 29133 encoding RT four genes of the oxidative pentose phosphate cycle."; RL Plant Physiol. 107:267-268(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102; RX PubMed=23463784; DOI=10.1104/pp.112.213116; RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.; RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a RT Cyanobacterium-Plant Symbiosis."; RL Plant Physiol. 161:1984-1992(2013). 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_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:0000255|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:0000255|HAMAP-Rule:MF_00493}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00493, ECO:0000305}. 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; L32796; AAA50769.1; -; Genomic_DNA. DR EMBL; CP001037; ACC82403.1; -; Genomic_DNA. DR RefSeq; WP_012410370.1; NC_010628.1. DR AlphaFoldDB; P48983; -. DR SMR; P48983; -. DR STRING; 63737.Npun_F4024; -. DR EnsemblBacteria; ACC82403; ACC82403; Npun_F4024. DR KEGG; npu:Npun_F4024; -. DR eggNOG; COG0176; Bacteria. DR HOGENOM; CLU_050771_1_0_3; -. DR OrthoDB; 140919at2; -. DR PhylomeDB; P48983; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000001191; 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. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase. FT CHAIN 1..381 FT /note="Transaldolase 2" FT /id="PRO_0000173629" FT ACT_SITE 110 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT ACT_SITE 141 FT /note="Nucleophile; Schiff-base intermediate with FT substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 19 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 46 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 141 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 163 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 202 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" FT BINDING 207 FT /ligand="D-fructose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61527" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493" SQ SEQUENCE 381 AA; 42303 MW; 906E28CDE77755F9 CRC64; MSTNHLLEIK QYGQSIWMDN LTRDIIQSGE LKDMVENQGI SGITSNPAIF EKAIAGNAIY DADIEAGVRA GLPIYKIYES LVFADIRNAC DILRPVYEAS NRLDGYVSIE VPPTIAHDTE ATISEARRYF QEIGRENLMI KIPGTEPGLP AVEQVIAEGM NVNITLLFSV ESYVNTAWAY VRGLEKRLAE GKDISRIASV ASFFLSRIDS NIDAKIDAKL KKGVDDIAVE AKLKAVKGKV AIANAKLAYQ EYKKIIRSER WQELVAKGAT VQRLLWASTS TKDPNYNDVM YIEELVGPDT VNTVPPATIK ACADHCNVSD RLETDVNNAY TLIENLKDPD INIDLDTVMD ELLVEGIDKF IQPFQSLMNS LEDKIKVLSP V //