TAL_PSEA7
ID TAL_PSEA7 Reviewed; 307 AA.
AC A6V3U3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=PSPA7_2361;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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_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; CP000744; ABR86225.1; -; Genomic_DNA.
DR RefSeq; WP_012075288.1; NC_009656.1.
DR AlphaFoldDB; A6V3U3; -.
DR SMR; A6V3U3; -.
DR EnsemblBacteria; ABR86225; ABR86225; PSPA7_2361.
DR KEGG; pap:PSPA7_2361; -.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001582; Chromosome.
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_1000014511"
FT ACT_SITE 125
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ SEQUENCE 307 AA; 33961 MW; 76D0477F0605E461 CRC64;
MTSKLEQLKQ YTTVVADTGD FDAIARLKPV DATTNPSLLL KAAALPRYAE HLRRATAGSG
GDAGLACDRF AVAVGKDILG VIPGRISTEV DARLSFDSEA TLARAHRLVE LYEEQGVGRE
RVLIKIASTW EGIRAAEILE REGIQTNLTL LFSFAQAAAC ADAGVFLISP FVGRIYDWYR
KSENRDYVGA EDPGVRSVSR IYRYYKANGY KTVVMGASFR NLGQIEQLAG CDRLTISPDL
LQQLADSQGE LPRLLLPGDG EPRQVLDESA FRWQMNEDAM ATEKLAEGIR LFARDQEKLE
YQLATRH