ID   TAL_MYCTO               Reviewed;         373 AA.
AC   P9WG32; L0T6W3; O06812;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=MT1495;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45758.1; -; Genomic_DNA.
DR   PIR; C70917; C70917.
DR   RefSeq; WP_003407447.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WG32; -.
DR   SMR; P9WG32; -.
DR   EnsemblBacteria; AAK45758; AAK45758; MT1495.
DR   KEGG; mtc:MT1495; -.
DR   PATRIC; fig|83331.31.peg.1607; -.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001020; 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; -; 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   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR   TIGRFAMs; TIGR00876; tal_mycobact; 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..373
FT                   /note="Transaldolase"
FT                   /id="PRO_0000428432"
FT   ACT_SITE        143
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  40691 MW;  CDB659CE154CF1E6 CRC64;
     MTAQNPNLAA LSAAGVSVWL DDLSRDRLRS GNLQELIDTK SVVGVTTNPS IFQKALSEGH
     TYDAQIAELA ARGADVDATI RTVTTDDVRS ACDVLVPQWE DSDGVDGRVS IEVDPRLAHE
     TEKTIQQAIE LWKIVDRPNL FIKIPATKAG LPAISAVLAE GISVNVTLIF SVQRYREVMD
     AYLTGMEKAR QAGHSLSKIH SVASFFVSRV DTEIDKRLDR IGSRQALELR GQAGVANARL
     AYAAYREVFE DSDRYRSLKV DGARVQRPLW ASTGVKNPDY SDTLYVTELV APHTVNTMPE
     KTIDAVADHG VIQGDTVTGT ASDAQAVFDQ LGAIGIDLTD VFAVLEEEGV RKFEASWNEL
     LQETRAHLDT AAQ