ID   TAL_MYCLB               Reviewed;         375 AA.
AC   B8ZUQ2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=MLBr00582;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00493}.
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         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}.
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DR   EMBL; FM211192; CAR70675.1; -; Genomic_DNA.
DR   RefSeq; WP_010907817.1; NC_011896.1.
DR   AlphaFoldDB; B8ZUQ2; -.
DR   SMR; B8ZUQ2; -.
DR   EnsemblBacteria; CAR70675; CAR70675; MLBr00582.
DR   KEGG; mlb:MLBr00582; -.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000006900; 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..375
FT                   /note="Transaldolase"
FT                   /id="PRO_1000198459"
FT   ACT_SITE        145
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   375 AA;  40588 MW;  10FCFB4765D665AB CRC64;
     MTSKIQNPNL AALSAAGVSV WLDDLSRDRL QSGNLQKLID TKSVVGVTTN PSIFQKAFAN
     GHAYDAQIAE LAKRGANVDV TVRTVTTDDV RHACDVLACE WEASHGKDGR VSIEVDPRLA
     HDTDKTIAQA VELWRIVDHP NLFIKIPATK AGLPAITAVL AEGISVNVTL IFSVQRHREV
     IDAYLAGIEK AAEAGRDLSK IVSVASFFVS RVDTEIDKRL EKLGSEQALA LRGQAGVANA
     RLAYAAYQKA FEGGQRYQTL MARGAQVQRP LWASTGVKNP DYADTLYVTE LVAPNTVNTM
     PETTIDAVAD HGVIRGDTIS GTTLSSQKVF DSLVAVGVDL IDVFAVLEHE GVQKFVKSWN
     ELLKETQEQL DSVAK