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Database: UniProt
Entry: Q9AIY4_CARRU
LinkDB: Q9AIY4_CARRU
Original site: Q9AIY4_CARRU 
ID   Q9AIY4_CARRU            Unreviewed;       297 AA.
AC   Q9AIY4;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=transaldolase {ECO:0000256|ARBA:ARBA00013151};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151};
GN   Name=tal {ECO:0000313|EMBL:AAK15390.1};
OS   Carsonella ruddii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=114186 {ECO:0000313|EMBL:AAK15390.1};
RN   [1] {ECO:0000313|EMBL:AAK15390.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10877784; DOI=10.1128/AEM.66.7.2898-2905.2000;
RA   Thao M.L., Moran N.A., Abbot P., Brennan E.B., Burckhardt D.H., Baumann P.;
RT   "Cospeciation of psyllids and their primary prokaryotic endosymbionts.";
RL   Appl. Environ. Microbiol. 66:2898-2905(2000).
RN   [2] {ECO:0000313|EMBL:AAK15390.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11222582; DOI=10.1128/JB.183.6.1853-1861.2001;
RA   Clark M.A., Baumann L., Thao M.L., Moran N.A., Baumann P.;
RT   "Degenerative minimalism in the genome of a psyllid endosymbiont.";
RL   J. Bacteriol. 183:1853-1861(2001).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518}.
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:0000256|ARBA:ARBA00001469};
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:0000256|ARBA:ARBA00004857}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012}.
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DR   EMBL; AF211141; AAK15390.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9AIY4; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   297 AA;  34256 MW;  32C5E409955C55A8 CRC64;
     MKFFDFIKNK TKISIDSADI NFIKNKLFNA ATTNPSLILK SILSKVYNKL LYAFLLKNFK
     KKIIDSDYNI SLYDKLLVNI IANIIPYIEE KISIEIPARI SFNYNKIIFY SYKIIYLCEK
     IGINLKKILI KIPATNSGIK AAKQLKNNNI NSNLTLIFNL TQAKKCFDSG IYIISPFVGR
     VSDSIYCKYD SGVNFVKNLV NLKNNNNYST KIMAASFRNI NQIINLTCCD FITISPIYYN
     KLKNINYKNS VLNYKSNIDF CNNENYNSIK LLNNGIKQFD IDHNRLIKLI SNLINNL
//
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