ID   TAL_DEHM1               Reviewed;         216 AA.
AC   Q3Z6N2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Probable transaldolase {ECO:0000255|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00494}; OrderedLocusNames=DET1409;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00494}.
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_00494};
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_00494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00494}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00494}.
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DR   EMBL; CP000027; AAW39333.1; -; Genomic_DNA.
DR   RefSeq; WP_010937094.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z6N2; -.
DR   SMR; Q3Z6N2; -.
DR   STRING; 243164.DET1409; -.
DR   EnsemblBacteria; AAW39333; AAW39333; DET1409.
DR   GeneID; 60795266; -.
DR   KEGG; det:DET1409; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_0; -.
DR   OMA; VRHPMHV; -.
DR   OrthoDB; 784333at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008289; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00494; Transaldolase_3b; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR022999; Transaldolase_3B.
DR   InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..216
FT                   /note="Probable transaldolase"
FT                   /id="PRO_1000126305"
FT   ACT_SITE        85
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   216 AA;  23305 MW;  AFEDE814BADD3BC9 CRC64;
     MRIFLDTANI EEIKKGLKLG VVSGVTTNPT LVAKEGISDY KSVVQQICAL LPEGDVSAEI
     TAEDPAEMLK QAREIAKWAP NVVVKIPATA EGLEIISKLS KEGVRFNMTL CFSVNQALLG
     ALAGAAFVSP FVGRLDDAGH DGMMLINDIV SIYKEYGFET QVIAASIRHP LHCTQAAQTG
     AGIATVPYKV LMQMMQHPLT DSGIARFMAD WKSVQK