ID   TAL_HELPS               Reviewed;         316 AA.
AC   B2UVP1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, 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=HPSH_07660;
OS   Helicobacter pylori (strain Shi470).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=512562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shi470;
RA   Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT   "Genome sequence of Helicobacter pylori from the remote Amazon: traces of
RT   Asian ancestry of the first Americans.";
RL   Submitted (MAY-2008) 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; CP001072; ACD48923.1; -; Genomic_DNA.
DR   RefSeq; WP_001155056.1; NC_010698.2.
DR   AlphaFoldDB; B2UVP1; -.
DR   SMR; B2UVP1; -.
DR   KEGG; hps:HPSH_07660; -.
DR   HOGENOM; CLU_050771_1_0_7; -.
DR   OMA; ATECYYQ; -.
DR   UniPathway; UPA00115; UER00414.
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; Schiff base; Transferase.
FT   CHAIN           1..316
FT                   /note="Transaldolase"
FT                   /id="PRO_1000126266"
FT   ACT_SITE        127
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   316 AA;  35215 MW;  B0D229D57B0A79DB CRC64;
     MQEFSLWCDF IERDFLENDF LKLINKGAIC GATSNPSLFC EAITKSAFYK DEIAKLKGKK
     AKEIYETLAL KDILQASSAL MPLYEKDPNN GYISLEIDPF LEDDAPKSID EAKRLFKTLN
     RPNVMIKVPA SESGLEVVSA LTKASIPVNA TLVFSPKIAR KTAQILAKEA QKRAVISVFV
     SRFDKEIDPL VPKNLQAKSG IINATECYYQ INQHANKLTS ALFASTGVKS NTLAKGYYIK
     ALCFKNSINT APLEALNAYL LDPNTEYQTP LKITEIEAFK KELKACNIDL ENTAQKLLKE
     GLIAFKQSFE KLLSSF