ID   TALB_ECOLI              Reviewed;         317 AA.
AC   P0A870; P30148;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Transaldolase B;
DE            EC=2.2.1.2 {ECO:0000269|PubMed:7592346};
GN   Name=talB; Synonyms=yaaK; OrderedLocusNames=b0008, JW0007;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   SUBUNIT.
RX   PubMed=7592346; DOI=10.1128/jb.177.20.5930-5936.1995;
RA   Sprenger G.A., Schorken U., Sprenger G., Sahm H.;
RT   "Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and
RT   characterization of the enzyme from recombinant strains.";
RL   J. Bacteriol. 177:5930-5936(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Iida A., Teshiba S., Mizobuchi K.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   0-2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA   Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL   Submitted (SEP-1994) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-13.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [8]
RP   PRESENCE OF TWO TRANSALDOLASES IN E.COLI.
RA   Sprenger G.A.;
RL   Unpublished observations (JUN-1993).
RN   [9] {ECO:0007744|PDB:1ONR}
RP   X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS), AND SUBUNIT.
RX   PubMed=8805555; DOI=10.1016/s0969-2126(96)00077-9;
RA   Jia J., Huang W., Schoerken U., Sham H., Sprenger G.A., Lindqvist Y.,
RA   Schneider G.;
RT   "Crystal structure of transaldolase B from Escherichia coli suggests a
RT   circular permutation of the alpha/beta barrel within the class I aldolase
RT   family.";
RL   Structure 4:715-724(1996).
RN   [10] {ECO:0007744|PDB:1UCW}
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=9007983; DOI=10.1002/pro.5560060113;
RA   Jia J., Schorken U., Lindqvist Y., Sprenger G.A., Schneider G.;
RT   "Crystal structure of the reduced Schiff-base intermediate complex of
RT   transaldolase B from Escherichia coli: mechanistic implications for class I
RT   aldolases.";
RL   Protein Sci. 6:119-124(1997).
RN   [11] {ECO:0007744|PDB:1I2N, ECO:0007744|PDB:1I2O, ECO:0007744|PDB:1I2P, ECO:0007744|PDB:1I2Q, ECO:0007744|PDB:1I2R}
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND ACTIVE SITE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=11298760; DOI=10.1046/j.1432-1327.2001.02128.x;
RA   Schorken U., Thorell S., Schurmann M., Jia J., Sprenger G.A., Schneider G.;
RT   "Identification of catalytically important residues in the active site of
RT   Escherichia coli transaldolase.";
RL   Eur. J. Biochem. 268:2408-2415(2001).
RN   [12] {ECO:0007744|PDB:3CWN}
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-316 OF MUTANT TYR-178, FUNCTION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF PHE-178.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=18687684; DOI=10.1074/jbc.m803184200;
RA   Schneider S., Sandalova T., Schneider G., Sprenger G.A., Samland A.K.;
RT   "Replacement of a phenylalanine by a tyrosine in the active site confers
RT   fructose-6-phosphate aldolase activity to the transaldolase of Escherichia
RT   coli and human origin.";
RL   J. Biol. Chem. 283:30064-30072(2008).
RN   [13] {ECO:0007744|PDB:3KOF}
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=20148428; DOI=10.1002/cbic.200900720;
RA   Schneider S., Gutierrez M., Sandalova T., Schneider G., Clapes P.,
RA   Sprenger G.A., Samland A.K.;
RT   "Redesigning the active site of transaldolase TalB from Escherichia coli:
RT   new variants with improved affinity towards nonphosphorylated substrates.";
RL   ChemBioChem 11:681-690(2010).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000269|PubMed:18687684,
CC       ECO:0000269|PubMed:7592346}.
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:0000269|PubMed:18687684, ECO:0000269|PubMed:7592346};
CC   -!- ACTIVITY REGULATION: Inhibited by Tris-HCl and phosphate buffer. Also
CC       competitively inhibited by sugars with L configuration at C2, such as
CC       D-arabinose-5-phosphate and L-glyceraldehyde.
CC       {ECO:0000269|PubMed:7592346}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=38 uM for D,L-glyceraldehyde 3-phosphate (with C3 acceptor
CC         compounds at pH 8.5 and 30 degrees Celsius)
CC         {ECO:0000269|PubMed:7592346};
CC         KM=90 uM for D-erythrose-4-phosphate (with C3 acceptor compounds at
CC         pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346};
CC         KM=31 mM for D-ribose-5-phosphate (with C3 acceptor compounds at pH
CC         8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346};
CC         KM=28 mM for D-glyceraldehyde (with C3 acceptor compounds at pH 8.5
CC         and 30 degrees Celsius) {ECO:0000269|PubMed:7592346};
CC         KM=285 uM for D-sedoheptulose-7-phosphate (with C3 donor compounds at
CC         pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346};
CC         KM=1200 uM for D-fructose-6-phosphate (with C3 donor compounds at pH
CC         8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:7592346};
CC         KM=3 mM for D-fructose-6-phosphate {ECO:0000269|PubMed:18687684};
CC         Vmax=85 umol/min/mg enzyme {ECO:0000269|PubMed:18687684};
CC         Note=kcat is 53 sec(-1) for D-fructose-6-phosphate.
CC         {ECO:0000269|PubMed:18687684};
CC       pH dependence:
CC         Optimum pH is between 8.5 and 9.5. {ECO:0000269|PubMed:7592346};
CC       Temperature dependence:
CC         Optimum temperature is between 15 and 40 degrees Celsius. At
CC         temperatures above 50 degrees Celsius, activity is lost rapidly, and
CC         at 55 degrees Celsius, the enzyme is totally inactivated.
CC         {ECO:0000269|PubMed:7592346};
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18687684,
CC       ECO:0000269|PubMed:7592346, ECO:0000269|PubMed:8805555}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Mutagenesis of Phe-178 to Tyr increases its preference
CC       for fructose-6-phosphate over 70-fold. {ECO:0000269|PubMed:18687684}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Transaldolase B entry;
CC       URL="https://en.wikipedia.org/wiki/Transaldolase_B";
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DR   EMBL; D13161; BAA21822.1; -; Genomic_DNA.
DR   EMBL; S80045; AAB47022.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73119.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96586.1; -; Genomic_DNA.
DR   PIR; S40535; S40535.
DR   RefSeq; NP_414549.1; NC_000913.3.
DR   RefSeq; WP_000130185.1; NZ_STEB01000033.1.
DR   PDB; 1I2N; X-ray; 2.05 A; A/B=2-317.
DR   PDB; 1I2O; X-ray; 2.05 A; A/B=2-317.
DR   PDB; 1I2P; X-ray; 2.05 A; A/B=2-317.
DR   PDB; 1I2Q; X-ray; 2.05 A; A/B=2-317.
DR   PDB; 1I2R; X-ray; 2.10 A; A/B=2-317.
DR   PDB; 1ONR; X-ray; 1.87 A; A/B=2-317.
DR   PDB; 1UCW; X-ray; 2.20 A; A/B=1-317.
DR   PDB; 3CWN; X-ray; 1.40 A; A/B=1-317.
DR   PDB; 3KOF; X-ray; 1.90 A; A/B=1-317.
DR   PDB; 4RZ5; X-ray; 1.80 A; A/B=1-317.
DR   PDB; 4RZ6; X-ray; 1.80 A; A/B=1-317.
DR   PDB; 4S2B; X-ray; 1.46 A; A/B=1-317.
DR   PDB; 4S2C; X-ray; 2.20 A; A/B=1-317.
DR   PDBsum; 1I2N; -.
DR   PDBsum; 1I2O; -.
DR   PDBsum; 1I2P; -.
DR   PDBsum; 1I2Q; -.
DR   PDBsum; 1I2R; -.
DR   PDBsum; 1ONR; -.
DR   PDBsum; 1UCW; -.
DR   PDBsum; 3CWN; -.
DR   PDBsum; 3KOF; -.
DR   PDBsum; 4RZ5; -.
DR   PDBsum; 4RZ6; -.
DR   PDBsum; 4S2B; -.
DR   PDBsum; 4S2C; -.
DR   AlphaFoldDB; P0A870; -.
DR   SMR; P0A870; -.
DR   BioGRID; 4261939; 9.
DR   BioGRID; 849151; 1.
DR   DIP; DIP-31850N; -.
DR   IntAct; P0A870; 9.
DR   STRING; 511145.b0008; -.
DR   jPOST; P0A870; -.
DR   PaxDb; 511145-b0008; -.
DR   EnsemblBacteria; AAC73119; AAC73119; b0008.
DR   GeneID; 83578047; -.
DR   GeneID; 944748; -.
DR   KEGG; ecj:JW0007; -.
DR   KEGG; eco:b0008; -.
DR   PATRIC; fig|1411691.4.peg.2275; -.
DR   EchoBASE; EB1517; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   InParanoid; P0A870; -.
DR   OMA; THAEFLW; -.
DR   OrthoDB; 9809101at2; -.
DR   PhylomeDB; P0A870; -.
DR   BioCyc; EcoCyc:TRANSALDOLB-MONOMER; -.
DR   BioCyc; MetaCyc:TRANSALDOLB-MONOMER; -.
DR   BRENDA; 2.2.1.2; 2026.
DR   UniPathway; UPA00115; UER00414.
DR   EvolutionaryTrace; P0A870; -.
DR   PRO; PR:P0A870; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004801; F:transaldolase activity; IDA:UniProtKB.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:EcoCyc.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
DR   SWISS-2DPAGE; P0A870; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Pentose shunt;
KW   Reference proteome; Schiff base; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7592346,
FT                   ECO:0000269|PubMed:9298646, ECO:0000269|Ref.6"
FT   CHAIN           2..317
FT                   /note="Transaldolase B"
FT                   /id="PRO_0000173593"
FT   ACT_SITE        132
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000269|PubMed:11298760"
FT   MUTAGEN         178
FT                   /note="F->Y: Critical for gain of fructose-6-phosphate
FT                   aldolase activity."
FT                   /evidence="ECO:0000269|PubMed:18687684"
FT   HELIX           4..8
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          12..17
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           21..27
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           36..43
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           49..62
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           66..86
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           105..121
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           137..148
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          153..158
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           161..169
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          173..179
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           180..189
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           201..215
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          221..225
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           230..235
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   TURN            236..238
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          239..244
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           246..254
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           278..286
FT                   /evidence="ECO:0007829|PDB:3CWN"
FT   HELIX           289..314
FT                   /evidence="ECO:0007829|PDB:3CWN"
SQ   SEQUENCE   317 AA;  35219 MW;  2DF03D741E576C31 CRC64;
     MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK
     QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN
     DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
     RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD
     RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
     KFAIDQEKLE KMIGDLL
//