ID   TAL_THISH               Reviewed;         373 AA.
AC   B8GMX9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Tgr7_2719;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73794.1; -; Genomic_DNA.
DR   RefSeq; WP_012639269.1; NC_011901.1.
DR   AlphaFoldDB; B8GMX9; -.
DR   SMR; B8GMX9; -.
DR   STRING; 396588.Tgr7_2719; -.
DR   PRIDE; B8GMX9; -.
DR   EnsemblBacteria; ACL73794; ACL73794; Tgr7_2719.
DR   KEGG; tgr:Tgr7_2719; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_6; -.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002383; 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; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..373
FT                   /note="Transaldolase"
FT                   /id="PRO_1000198460"
FT   ACT_SITE        144
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   373 AA;  40944 MW;  0C647DE1CAD4CF97 CRC64;
     MSAENRIRAL RALGQSIWYD YIRRDLLDSG ELARLIREDG LGGLTSNPAI FDKAIAGTDL
     YRTAIRDALR ADPGLNDEAL FFRLAIEDLQ RAADVFLPLY RETGGADGFV SLEVSPDLAH
     DAEATVREAR ALFARMDRPN AMIKVPGTRA GVEALETLIA DGVNVNVTLL FSVARYAQVL
     EAWMRGMEAR LERGEALETV TSVASFFVSR VDSVLDPLLE ERIQEGRPAE HLRGRLAIAN
     ARLAYAHFRD QRGGARHTRL TAAGAHPQRL LWASTGTKNP DYSDVLYVDS LIGEHTVNTL
     PPATYRAFLD HGSVAETLAE GVETARAQVA ALADLGIDLE SITDRLESEG IEAFQKAFRH
     LLGVLAEARQ GKR