TAL_PSEA8
ID TAL_PSEA8 Reviewed; 307 AA.
AC B7UWP0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=PLES_22761;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
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_00492};
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_00492}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR EMBL; FM209186; CAW27003.1; -; Genomic_DNA.
DR RefSeq; WP_012613934.1; NC_011770.1.
DR AlphaFoldDB; B7UWP0; -.
DR SMR; B7UWP0; -.
DR PRIDE; B7UWP0; -.
DR KEGG; pag:PLES_22761; -.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OMA; KFGYKTL; -.
DR UniPathway; UPA00115; UER00414.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR10683:SF18; PTHR10683:SF18; 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; Schiff base; Transferase.
FT CHAIN 1..307
FT /note="Transaldolase"
FT /id="PRO_1000126251"
FT ACT_SITE 125
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ SEQUENCE 307 AA; 34005 MW; F51C2B6AF282ED41 CRC64;
MTSKLEQLKQ YTTVVADTGD FDAIARLKPV DATTNPSLLL KAAALPRYAE HLRQATAGSG
GDAGLACDRF AVAVGKDILG VIPGRISTEV DARLSFDSEA TLARAHRLIE LYDEQGIDRE
RVLIKIASTW EGIRAAEILE REGIQTNLTL LFSFAQAVAC ADAGVFLISP FVGRIYDWYK
KSENRDYVGA EDPGVQSVSR IYRYYKANGY KTVVMGASFR NLGQIEQLAG CDRLTISPDL
LQQLADAQGE LPRLLLPGEG EPRQVLDEST FRWQMNEDAM ATEKLAEGIR LFARDQEKLE
YQLATRH
