ID   TAL_PSECP               Reviewed;         371 AA.
AC   B8H7N3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Achl_1837;
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC   13794 / A6;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001341; ACL39813.1; -; Genomic_DNA.
DR   RefSeq; WP_015937033.1; NC_011886.1.
DR   AlphaFoldDB; B8H7N3; -.
DR   SMR; B8H7N3; -.
DR   STRING; 452863.Achl_1837; -.
DR   EnsemblBacteria; ACL39813; ACL39813; Achl_1837.
DR   KEGG; ach:Achl_1837; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_050771_1_0_11; -.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002505; 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; Schiff base; Transferase.
FT   CHAIN           1..371
FT                   /note="Transaldolase"
FT                   /id="PRO_1000198457"
FT   ACT_SITE        140
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   371 AA;  39528 MW;  01CAB26803F68AB2 CRC64;
     MTTPTQQLSE AGVSIWLDDL SRGRLETGTL RKLIEEKNVV GVTTNPSIFH AAITAGTDYD
     ATVAAQAAAG ASVEETIFEI TTTDVADACD LFAPVAAATK GVDGRVSIEV DPRLAWDTNG
     TIAEAKHLYK KVNKDNVLIK IPATIEGLEA ITATLAEGIS VNVTLIFSLE RYRAVINAFQ
     AGLEQAKENG HDLSKIHSVA SFFVSRVDSE IDKRLDKIGT DEAKALKGKA GLANARLAYQ
     VYEELFATER WALLAEAGAL PQRPLWASTG VKDPAYPDTL YVTELVAPGV VNTMPEKTLD
     ATFDHGVVTG DTVSGTYADA NATLDALEKL GVSYNEVVAL LESEGLDKFV ASWKELLADV
     EGALASARKA S