ID   TAL_TRIV2               Reviewed;         332 AA.
AC   P51778; Q3MFW9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=Ava_0493;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8616240; DOI=10.1007/bf00017817;
RA   Koehler U., Cerff R., Brinkmann H.;
RT   "Transaldolase genes from the cyanobacteria Anabaena variabilis and
RT   Synechocystis sp. PCC 6803: comparison with other eubacterial and
RT   eukaryotic homologues.";
RL   Plant Mol. Biol. 30:213-218(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
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_00492};
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_00492}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00492, ECO:0000305}.
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DR   EMBL; L47327; AAC41527.1; -; Genomic_DNA.
DR   EMBL; CP000117; ABA20117.1; -; Genomic_DNA.
DR   PIR; S72517; S72517.
DR   AlphaFoldDB; P51778; -.
DR   SMR; P51778; -.
DR   STRING; 240292.Ava_0493; -.
DR   EnsemblBacteria; ABA20117; ABA20117; Ava_0493.
DR   KEGG; ava:Ava_0493; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_0_3; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..332
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173578"
FT   ACT_SITE        136
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
FT   CONFLICT        204
FT                   /note="D -> Y (in Ref. 1; AAC41527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="T -> S (in Ref. 1; AAC41527)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   332 AA;  36165 MW;  3536377CFEA0D692 CRC64;
     MTKNLLEQLR EMTVVVADTG DIQAIEKFTP RDATTNPSLI TAAAKMPEYQ EIVDQTLLQA
     KKDAGAGASK GQIVSLAFDR LAVSFGLKIL QIIPGRVSTE VDARLSYDTE ATITKARELI
     AQYKAAGIGP ERVLIKIAST WEGIKAAEIL EKEGIHCNLT LLFGLHQAIA CAEAGITLIS
     PFVGRILDWY KKETGRDSYP SAEDPGVISV TTIYNYYKKF GYTTEVMGAS FRNIGEITEL
     AGSDLLTISP GLLGELQATI GELPRKLDPA KAATLDIEKI SIDKATFDKM HAADRMAYDK
     LDEGIKGFTK ALEELETLLA ERLARLEVVA SH