ID   TAL_MYCTU               Reviewed;         373 AA.
AC   P9WG33; L0T6W3; O06812;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=Rv1448c; ORFNames=MTCY493.06;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44207.1; -; Genomic_DNA.
DR   PIR; C70917; C70917.
DR   RefSeq; NP_215964.1; NC_000962.3.
DR   RefSeq; WP_003912809.1; NZ_NVQJ01000071.1.
DR   AlphaFoldDB; P9WG33; -.
DR   SMR; P9WG33; -.
DR   STRING; 83332.Rv1448c; -.
DR   PaxDb; P9WG33; -.
DR   DNASU; 886606; -.
DR   GeneID; 886606; -.
DR   KEGG; mtu:Rv1448c; -.
DR   TubercuList; Rv1448c; -.
DR   eggNOG; COG0176; Bacteria.
DR   OMA; ATECYYQ; -.
DR   PhylomeDB; P9WG33; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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   1: Evidence at protein level;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..373
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173636"
FT   ACT_SITE        143
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  40721 MW;  8CBA28D2654CF1FA 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
     AYATYREVFE DSDRYRSLKV DGARVQRPLW ASTGVKNPDY SDTLYVTELV APHTVNTMPE
     KTIDAVADHG VIQGDTVTGT ASDAQAVFDQ LGAIGIDLTD VFAVLEEEGV RKFEASWNEL
     LQETRAHLDT AAQ