ID   TAL2_NOSS1              Reviewed;         381 AA.
AC   P48993;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Transaldolase 2;
DE            EC=2.2.1.2;
GN   Name=tal2; OrderedLocusNames=all4020;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8566707; DOI=10.1111/j.1574-6968.1995.tb07882.x;
RA   Newman J., Karakaya H., Scanlan D.J., Mann N.H.;
RT   "A comparison of gene organization in the zwf region of the genomes of the
RT   cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120.";
RL   FEMS Microbiol. Lett. 133:187-193(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; U33282; AAA98852.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB75719.1; -; Genomic_DNA.
DR   PIR; AE2308; AE2308.
DR   RefSeq; WP_010998160.1; NZ_RSCN01000023.1.
DR   AlphaFoldDB; P48993; -.
DR   SMR; P48993; -.
DR   STRING; 103690.17133155; -.
DR   EnsemblBacteria; BAB75719; BAB75719; BAB75719.
DR   KEGG; ana:all4020; -.
DR   eggNOG; COG0176; Bacteria.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002483; 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 2"
FT                   /id="PRO_0000173628"
FT   ACT_SITE        141
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15..16
FT                   /note="SI -> MY (in Ref. 1; AAA98852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  42023 MW;  1A016AD8B486311A CRC64;
     MAINHLLEIK EYGQSIWMDN LSRDIIQSGE LKNLVENQGI CGITSNPAIF EKAIANNVIY
     DADIEAGVRA GLPTYKIYES LIFADIRNAC DILRPVYEAS NKLDGYVSIE VPPTIAHDTQ
     ATINEARRYY QEIGRENVMI KIPGTEAGLP AVEQVIAEGI NVNVTLLFSV QSYINTIWAY
     IRGLEKRLAE GKDISQIASV ASFFLSRIDI NIDGKIDAKL ARGVDDISLE AKLMVVKGKV
     AIANAKIAYQ EYKKIIESDQ WQALAAKGAK VQRLLWASTS TKDPNYSDVM YVDELIGPDT
     VNTLPPATIT ACADHCEVAN RVETGVAEAY QLIESLKDPD INIDINAVMD ELLIEGINKF
     VQPFQSLMNS LEGKVKLLSP V