TALA_ECOLI
ID TALA_ECOLI Reviewed; 316 AA.
AC P0A867; P78258; P80218;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transaldolase A;
DE EC=2.2.1.2;
GN Name=talA; OrderedLocusNames=b2464, JW2448;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP PRESENCE OF TWO TRANSALDOLASES IN E.COLI.
RA Sprenger G.A.;
RL Unpublished observations (JUN-1993).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; D13159; BAA21821.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75517.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16339.1; -; Genomic_DNA.
DR PIR; G65021; G65021.
DR RefSeq; NP_416959.1; NC_000913.3.
DR RefSeq; WP_001003709.1; NZ_STEB01000051.1.
DR AlphaFoldDB; P0A867; -.
DR SMR; P0A867; -.
DR BioGRID; 4260921; 12.
DR DIP; DIP-47872N; -.
DR IntAct; P0A867; 11.
DR STRING; 511145.b2464; -.
DR jPOST; P0A867; -.
DR PaxDb; P0A867; -.
DR PRIDE; P0A867; -.
DR EnsemblBacteria; AAC75517; AAC75517; b2464.
DR EnsemblBacteria; BAA16339; BAA16339; BAA16339.
DR GeneID; 66673675; -.
DR GeneID; 947006; -.
DR KEGG; ecj:JW2448; -.
DR KEGG; eco:b2464; -.
DR PATRIC; fig|1411691.4.peg.4276; -.
DR EchoBASE; EB1745; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_6; -.
DR InParanoid; P0A867; -.
DR OMA; DTGDFKQ; -.
DR PhylomeDB; P0A867; -.
DR BioCyc; EcoCyc:TRANSALDOLA-MON; -.
DR UniPathway; UPA00115; UER00414.
DR PRO; PR:P0A867; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00874; talAB; 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 A"
FT /id="PRO_0000173590"
FT ACT_SITE 131
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 35659 MW; 990B00ED7937CF19 CRC64;
MNELDGIKQF TTVVADSGDI ESIRHYHPQD ATTNPSLLLK AAGLSQYEHL IDDAIAWGKK
NGKTQEQQVV AACDKLAVNF GAEILKIVPG RVSTEVDARL SFDKEKSIEK ARHLVDLYQQ
QGVEKSRILI KLASTWEGIR AAEELEKEGI NCNLTLLFSF AQARACAEAG VFLISPFVGR
IYDWYQARKP MDPYVVEEDP GVKSVRNIYD YYKQHHYETI VMGASFRRTE QILALTGCDR
LTIAPNLLKE LQEKVSPVVR KLIPPSQTFP RPAPMSEAEF RWEHNQDAMA VEKLSEGIRL
FAVDQRKLED LLAAKL
