TAL_CAMJJ
ID TAL_CAMJJ Reviewed; 325 AA.
AC A1VY04;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00493};
GN OrderedLocusNames=CJJ81176_0307;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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_00493}.
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_00493};
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_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00493}.
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DR EMBL; CP000538; EAQ73014.1; -; Genomic_DNA.
DR RefSeq; WP_002857444.1; NC_008787.1.
DR AlphaFoldDB; A1VY04; -.
DR SMR; A1VY04; -.
DR STRING; 354242.CJJ81176_0307; -.
DR EnsemblBacteria; EAQ73014; EAQ73014; CJJ81176_0307.
DR KEGG; cjj:CJJ81176_0307; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_7; -.
DR OMA; ATECYYQ; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004732; Transaldolase_2.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR TIGRFAMs; TIGR00876; tal_mycobact; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT CHAIN 1..325
FT /note="Transaldolase"
FT /id="PRO_1000026521"
FT ACT_SITE 125
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ SEQUENCE 325 AA; 36861 MW; D62EFCDD9C1E5F26 CRC64;
MKNFSLWCDF IENSFLDNEF LNLLSHGING ATSNPAIFKN AILNSPIYKD KILKLKGKKT
KDIYEELAIS DIQKAADKLA PLFYQKNDGF ISIEIDPRLH DNTTLSLGEA KRLYSAISKE
NVMIKIPATK ASYEVMYELM KNGISVNATL IFSLEQSQKC FEALNAGLVE FRKNNIALKE
QNTRTPQAVI SIFVSRFDRL LNPKAKEQNR IGILNANLAY NNIYSKNEPN IRALFASTGV
KGDDLPKDYY IKELLFENSV NTAPLDAIEA FKGKMHFKKP LMNFEIYTEL NQIISQSERE
KACNDLLSDG LEQFCIAFED ILKAL
