ID   TAL_MYCLE               Reviewed;         375 AA.
AC   P55193; O65930; Q49698; Q49705;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=ML0582;
GN   ORFNames=B1496_F2_65/B1496_F1_27, MLCL536.39;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=8616240; DOI=10.1007/bf00017817;
RA   Koehler U., Cerff R., Brinkmann H.;
RT   "Transaldolase genes from the cyanobacteria Anabaena variabilis and
RT   Synechocystis sp. PCC 6803: comparison with other eubacterial and
RT   eukaryotic homologues.";
RL   Plant Mol. Biol. 30:213-218(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17140.1; Type=Frameshift; Evidence={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; U00013; AAA17145.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00013; AAA17140.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; Z99125; CAB16183.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30090.1; -; Genomic_DNA.
DR   PIR; T11020; T11020.
DR   RefSeq; NP_301493.1; NC_002677.1.
DR   RefSeq; WP_010907817.1; NC_002677.1.
DR   AlphaFoldDB; P55193; -.
DR   SMR; P55193; -.
DR   STRING; 272631.ML0582; -.
DR   EnsemblBacteria; CAC30090; CAC30090; CAC30090.
DR   KEGG; mle:ML0582; -.
DR   PATRIC; fig|272631.5.peg.1016; -.
DR   Leproma; ML0582; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   OMA; ATECYYQ; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000806; 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; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..375
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173635"
FT   ACT_SITE        145
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        155
FT                   /note="A -> G (in Ref. 1)"
FT                   /evidence="ECO:0000305"
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