TAL_BACFR
ID TAL_BACFR Reviewed; 218 AA.
AC Q64R94;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=BF3242;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD49987.1; -; Genomic_DNA.
DR RefSeq; WP_005789246.1; NC_006347.1.
DR RefSeq; YP_100521.1; NC_006347.1.
DR AlphaFoldDB; Q64R94; -.
DR SMR; Q64R94; -.
DR STRING; 295405.BF3242; -.
DR EnsemblBacteria; BAD49987; BAD49987; BF3242.
DR KEGG; bfr:BF3242; -.
DR PATRIC; fig|295405.11.peg.3112; -.
DR HOGENOM; CLU_079764_0_0_10; -.
DR OMA; VRHPMHV; -.
DR BRENDA; 3.2.1.127; 755.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000002197; 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..218
FT /note="Probable transaldolase"
FT /id="PRO_1000126277"
FT ACT_SITE 87
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ SEQUENCE 218 AA; 23687 MW; BA401C18EF773A1B CRC64;
MKFFIDTANL DQIREAHDLG VLDGVTTNPS LMAKEGIKGV ENQRRHYVEI CNIVQGDVSA
EVIATDYEGM VREGKELAAL NPHIVVKVPC IADGIKAIKH FSGKGIRTNC TLVFSTGQAL
LAAKAGATYV SPFVGRLDDI CEDGVGLVAD IVRMYRFYNY PTQVLAASIR SSKHIMECVE
AGADVATCPL SAIKGLMNHP LTDAGLKKFL EDYKKVNE
