ID   TAL1_STRCO              Reviewed;         381 AA.
AC   O88018;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Transaldolase 1;
DE            EC=2.2.1.2;
GN   Name=tal1; Synonyms=tal; OrderedLocusNames=SCO6662; ORFNames=SC5A7.12c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250}.
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL939128; CAA19941.1; -; Genomic_DNA.
DR   PIR; T35161; T35161.
DR   RefSeq; NP_630737.1; NC_003888.3.
DR   RefSeq; WP_011031085.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; O88018; -.
DR   SMR; O88018; -.
DR   STRING; 100226.SCO6662; -.
DR   GeneID; 1102101; -.
DR   KEGG; sco:SCO6662; -.
DR   PATRIC; fig|100226.15.peg.6768; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   InParanoid; O88018; -.
DR   OMA; RMMTTAD; -.
DR   PhylomeDB; O88018; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001973; 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.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..381
FT                   /note="Transaldolase 1"
FT                   /id="PRO_0000173641"
FT   ACT_SITE        149
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  40407 MW;  44068BD43598F5B5 CRC64;
     MITVTEATAT AGALQRLADQ GVSVWLDDLS RRRIESGNLA ELIRTKNVVG VTTNPSIFQA
     AIGSGEGYEE QLADLATRGV TVDEAVRMMT TADVRAAADV LRGVYDASGG RDGRVSIEVD
     PRLAHDTAAT VAEARQLSWL VDRPNVMIKI PATKAGLPAI TEVIGAGISV NVTLIFSLER
     YREVMDAYLA GLEKAQAAGI DLAGIHSVAS FFVSRVDSEI DKRLSLLGTE EALGLRGRAA
     LANARLAYEA YENVFAGDRF TALAGARANA QRPLWASTGV KDPAFRDTLY VEELVAPGTV
     NTMPEATLDA AADHGDVRGD TVTGGYAQAR ADLAAVERLG VSYDEVVEQL EQEGVAKFEA
     AWQELLAAVT KSLDSKGVDG E