TAL_CLOBB
ID TAL_CLOBB Reviewed; 214 AA.
AC B2TKE5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=CLL_A1586;
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B;
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) 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; CP001056; ACD24413.1; -; Genomic_DNA.
DR RefSeq; WP_003372337.1; NC_018648.1.
DR AlphaFoldDB; B2TKE5; -.
DR SMR; B2TKE5; -.
DR EnsemblBacteria; ACD24413; ACD24413; CLL_A1586.
DR KEGG; cbk:CLL_A1586; -.
DR PATRIC; fig|935198.13.peg.1532; -.
DR HOGENOM; CLU_079764_0_0_9; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001195; 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; Schiff base; Transferase.
FT CHAIN 1..214
FT /note="Probable transaldolase"
FT /id="PRO_1000126294"
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ SEQUENCE 214 AA; 23212 MW; DE4AA70028484CF0 CRC64;
MKIFVDTANI EEIKKANELG VICGVTTNPS LIAKEGRDFK EVIKEITSIV DGPISGEVIS
MECEGMVKEA REIAKIHENM VIKIPMCAEG LKAVNILHKE GIKTNVTLIF SAVQALLAAR
AGASYVSPFL GRLDDIGSTG MTLIEDISEI FAVHGIETEI ISASVRNPIH VLECAKAGSD
IATIPYNVIM QMIKHPLTDA GIEKFLKDYE GMNK
