ID TALA_SALTY Reviewed; 316 AA. AC Q8ZN83; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 01-MAY-2007, entry version 28. DE Transaldolase A (EC 2.2.1.2). GN Name=talA; OrderedLocusNames=STM2473; OS Salmonella typhimurium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=602; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., RA Waterston R., Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium RT LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway (By similarity). CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC fructose 6-phosphate and D-glyceraldehyde 3-phosphate from D- CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative CC stage): step 2/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily. 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; AE008811; AAL21367.1; -; Genomic_DNA. DR HSSP; P30148; 1ONR. DR GenomeReviews; AE006468_GR; STM2473. DR KEGG; stm:STM2473; -. DR StyGene; SG?????; talA. DR BioCyc; STYP99287:STM2473-MONOMER; -. DR GO; GO:0004801; F:transaldolase activity; IEA:HAMAP. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP. DR HAMAP; MF_00492; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; Transaldolase. DR InterPro; IPR004730; Transaldolase_AB. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1. DR PANTHER; PTHR10683; Transaldolase; 1. DR PANTHER; PTHR10683:SF3; Transaldolase_AB; 1. DR Pfam; PF00923; Transaldolase; 1. DR PIRSF; PIRSF000419; Transaldolase; 1. DR TIGRFAMs; TIGR00874; talAB; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; FALSE_NEG. KW Complete proteome; Pentose shunt; Transferase. FT CHAIN 1 316 Transaldolase A. FT /FTId=PRO_0000173612. FT ACT_SITE 131 131 By similarity. SQ SEQUENCE 316 AA; 35592 MW; 7361CBB6C25A2386 CRC64; MNQLDGIKQF TTVVADSGDI ESIRHYQPQD ATTNPSLLLK AAGLEQYGHL IEDAIAWGKK HGGTQEQQVA AASDKLAVNF GAEILKSIPG RVSTEVDARL SFDKEKSIEK ARHLVDLYQQ QGVDKSRILI KLAATWEGIR AAGQLEKEGI NCNLTLLFSF AQARACAEAG VYLISPFVGR IYDWYQARSP LEPYVVEEDP GVKSVRNIYD YFKQHRYETI VMGASFRRTE QILALTGCDR LTISPNLLKE LKEKEEPVIR KLVPSSQMFH RPTPMTEAEF RWEHNQDAMA VEKLSEGIRL FAVDQRKLED LLAAKL //