ID   TAL_ARTS2               Reviewed;         371 AA.
AC   A0JWQ6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=Arth_2096;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24;
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00493}.
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_00493};
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_00493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00493}.
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DR   EMBL; CP000454; ABK03476.1; -; Genomic_DNA.
DR   RefSeq; WP_011691942.1; NC_008541.1.
DR   AlphaFoldDB; A0JWQ6; -.
DR   SMR; A0JWQ6; -.
DR   STRING; 290399.Arth_2096; -.
DR   PRIDE; A0JWQ6; -.
DR   EnsemblBacteria; ABK03476; ABK03476; Arth_2096.
DR   KEGG; art:Arth_2096; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000754; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..371
FT                   /note="Transaldolase"
FT                   /id="PRO_1000060453"
FT   ACT_SITE        140
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   371 AA;  39531 MW;  755D26AC17E60412 CRC64;
     MTTPTQQLSD AGVSIWLDDL SRGRLQTGTL RKLIEEKNVV GVTTNPSIFH AAITSGTDYD
     ATIAEQAAAG STVEETVFEI TTTDVADACD LFAPVAAATR GVDGRVSIEV DPRLAWDTAG
     TIAEAKHLYK KVNKDNVLIK IPATLEGLEA ITATLAEGIS VNVTLIFSLE RYRAVINAFQ
     SGLEQAKGNG HDLSKIHSVA SFFVSRVDAE IDKRLDAIGT DEAKALKGKA GLANARLAYQ
     VYEELFSTER WALLAEAGAL PQRPLWASTG VKDPSYPDTL YVTELVAPGV VNTMPEKTLD
     ATFDHGVVTG DTVTRGYDDA NATLNALDAL GISYNDVVAL LESEGLDKFV ASWKELLGDV
     EGALASARKA S