ID   TAL_MYCS2               Reviewed;         371 AA.
AC   A0QWX9; I7FL90;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=MSMEG_3102, MSMEI_3024;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-132, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250}.
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   -!- 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000480; ABK72383.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP39488.1; -; Genomic_DNA.
DR   RefSeq; WP_011728814.1; NZ_SIJM01000002.1.
DR   RefSeq; YP_887417.1; NC_008596.1.
DR   AlphaFoldDB; A0QWX9; -.
DR   SMR; A0QWX9; -.
DR   STRING; 246196.MSMEI_3024; -.
DR   EnsemblBacteria; ABK72383; ABK72383; MSMEG_3102.
DR   EnsemblBacteria; AFP39488; AFP39488; MSMEI_3024.
DR   GeneID; 66734505; -.
DR   KEGG; msg:MSMEI_3024; -.
DR   KEGG; msm:MSMEG_3102; -.
DR   PATRIC; fig|246196.19.peg.3063; -.
DR   eggNOG; COG0176; Bacteria.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Pentose shunt; Reference proteome; Schiff base;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..371
FT                   /note="Transaldolase"
FT                   /id="PRO_0000396810"
FT   ACT_SITE        142
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        132
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   371 AA;  39936 MW;  C24083E85016D640 CRC64;
     MAQNPNLAAL SAAGVSVWLD DLSRDRLQTG NLTELINTRS VVGVTTNPSI FQAALSKGTA
     YDAQVNELAA RGADVDATIR TVTTDDVRNA CDLLAKEYEA SDGVDGRVSI EVDPRLAHDT
     DKTILQAIEL WKIVDRPNLL IKIPATMAGL PAISAVIAEG ISVNVTLIFS VERHRLVMDA
     YLEGLEKAKE AGHDLSKIHS VASFFVSRVD TEIDARLEKI GSDEALALRG KAGVANARLA
     YAAYEEVFGS DRFAKLKADG ARVQRPLWAS TGVKNPEYSD TLYVTELVAP NTVNTMPEKT
     LEAVADHGEI TGNTIAGTAA SSQETFDKLA AIGIDLPDVF RVLEDEGVEK FEKSWQELLD
     ATQGQLDAAK K