ID   TAL_HELPY               Reviewed;         316 AA.
AC   P56108;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=HP_1495;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD08536.1; -; Genomic_DNA.
DR   PIR; G64706; G64706.
DR   RefSeq; NP_208286.1; NC_000915.1.
DR   RefSeq; WP_001155041.1; NC_018939.1.
DR   AlphaFoldDB; P56108; -.
DR   SMR; P56108; -.
DR   STRING; 85962.C694_07745; -.
DR   PaxDb; P56108; -.
DR   EnsemblBacteria; AAD08536; AAD08536; HP_1495.
DR   KEGG; hpy:HP_1495; -.
DR   PATRIC; fig|85962.47.peg.1607; -.
DR   eggNOG; COG0176; Bacteria.
DR   OMA; ATECYYQ; -.
DR   PhylomeDB; P56108; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000429; 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..316
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173631"
FT   ACT_SITE        127
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  35195 MW;  8CC7A0832EA657CD CRC64;
     MQEFSLWCDF IERDFLENDF LKLINKGAIC GATSNPSLFC EAITKSAFYK DEIAKLKGKK
     AKEIYETLAL KDILQASSAL MPLYEKDPNN GYISLEIDPF LEDDAAKSID EAKRLFKTLN
     RPNVMIKVPA SESGIEVVSA LTQASIPVNV TLVFSPKIAG EIAQILAKEA QKRAVISVFV
     SRFDKEIDPL VPKNLQAQSG IINATECYYQ INQHANKLTS TLFASTGVKS NSLAKDYYIK
     ALCFKNSINT APLEALNAYL LDPNTECQTP LKTTEIEAFK KELKVHNIDL ENTAQKLLKE
     GLIAFKQSFE KLLSSF