ID   TAL_PSEAE               Reviewed;         307 AA.
AC   Q9I047;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=PA2796;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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   -!- 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, ECO:0000305}.
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DR   EMBL; AE004091; AAG06184.1; -; Genomic_DNA.
DR   PIR; D83295; D83295.
DR   RefSeq; NP_251486.1; NC_002516.2.
DR   RefSeq; WP_003090868.1; NZ_QZGE01000011.1.
DR   AlphaFoldDB; Q9I047; -.
DR   SMR; Q9I047; -.
DR   STRING; 287.DR97_5147; -.
DR   PaxDb; Q9I047; -.
DR   PRIDE; Q9I047; -.
DR   DNASU; 882755; -.
DR   EnsemblBacteria; AAG06184; AAG06184; PA2796.
DR   GeneID; 882755; -.
DR   KEGG; pae:PA2796; -.
DR   PATRIC; fig|208964.12.peg.2934; -.
DR   PseudoCAP; PA2796; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   InParanoid; Q9I047; -.
DR   OMA; KFGYKTL; -.
DR   PhylomeDB; Q9I047; -.
DR   BioCyc; PAER208964:G1FZ6-2843-MON; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..307
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173607"
FT   ACT_SITE        125
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   307 AA;  33946 MW;  840B2B6AF2885B94 CRC64;
     MTSKLEQLKQ YTTVVADTGD FDAIARLKPV DATTNPSLLL KAAALPRYAE HLRQATAGSG
     GDAGLACDRF AVAVGKDILG VIPGRISTEV DARLSFDSEA TLARAHRLIE LYDEQGIDRE
     RVLIKIASTW EGIRAAEILE REGIQTNLTL LFSFAQAVAC ADAGVFLISP FVGRIYDWYK
     KSENRDYAGA EDPGVQSVSR IYRYYKANGY KTVVMGASFR NLGQIEQLAG CDRLTISPDL
     LQQLADAQGE LPRLLLPGEG EPRQVLDESA FRWQMNEDAM ATEKLAEGIR LFARDQEKLE
     YQLATRH