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TAL_CALS8
ID   TAL_CALS8               Reviewed;         217 AA.
AC   A4XL36;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Csac_2036;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA   VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA   Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA   Kengen S.M.W., Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000679; ABP67621.1; -; Genomic_DNA.
DR   RefSeq; WP_011917556.1; NC_009437.1.
DR   AlphaFoldDB; A4XL36; -.
DR   SMR; A4XL36; -.
DR   STRING; 351627.Csac_2036; -.
DR   EnsemblBacteria; ABP67621; ABP67621; Csac_2036.
DR   KEGG; csc:Csac_2036; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_9; -.
DR   OMA; VRHPMHV; -.
DR   OrthoDB; 784333at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000256; 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.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..217
FT                   /note="Probable transaldolase"
FT                   /id="PRO_1000060462"
FT   ACT_SITE        83
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   217 AA;  23735 MW;  55E899DBABBC0063 CRC64;
     MKLFIDTANI NEIKEAYSWG IICGVTTNPS LIAKEGRDFK EVVNEICSIV DGPISAEVIS
     LKAEGMIEEA RDLAKIHKNV VIKIPMTTEG LKAVSVLSKE GIKTNVTLIF SAAQALLAAK
     AGATYVSPFV GRLDDIGQNG IELIKEIVQI FRNYPDIKTE IIAASIRHPI HVIEAAKAGA
     DIATVPFKVL EQMTKHALTD IGIERFLKDW EKVPKKN
 
 
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