TAL_PSEE4
ID TAL_PSEE4 Reviewed; 308 AA.
AC Q1I7G7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=PSEEN3692;
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK16415.1; -; Genomic_DNA.
DR RefSeq; WP_011534792.1; NC_008027.1.
DR AlphaFoldDB; Q1I7G7; -.
DR SMR; Q1I7G7; -.
DR STRING; 384676.PSEEN3692; -.
DR EnsemblBacteria; CAK16415; CAK16415; PSEEN3692.
DR KEGG; pen:PSEEN3692; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000000658; 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..308
FT /note="Transaldolase"
FT /id="PRO_1000014513"
FT ACT_SITE 125
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ SEQUENCE 308 AA; 33765 MW; B5018E42EDCEE394 CRC64;
MTSKLEQLKQ FTTVVADTGD LDAITRLKPV DATTNPSLLL KAAAIPGYAD LLEQVKADTK
GNVDLACDKF AVSVGAGILK VIPGRISTEV DARLSFDEPA LLKKAHQLIE LYEAAGIKRD
RVLIKLASTW EGIRAAEKLE KEGIQTNLTL LFSFAQAQAC ADAGVFLISP FVGRIYDWYK
KSTGKEYIGA EDPGVQSVTR IYDYYKANGY NTVVMGASFR NIGQIEQLAG CDRLTISPEL
LVQLSDDQGE LPRILKPGNA GEAKQQLNES QFRWAMNEDA MATEKLAEGI RQFARDQEKL
EALMADKA