TAL_MYCTA
ID TAL_MYCTA Reviewed; 373 AA.
AC A5U2F1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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}; OrderedLocusNames=MRA_1457;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ73201.1; -; Genomic_DNA.
DR RefSeq; WP_003912809.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U2F1; -.
DR SMR; A5U2F1; -.
DR STRING; 419947.MRA_1457; -.
DR EnsemblBacteria; ABQ73201; ABQ73201; MRA_1457.
DR KEGG; mra:MRA_1457; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_11; -.
DR OMA; ATECYYQ; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001988; 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 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT CHAIN 1..373
FT /note="Transaldolase"
FT /id="PRO_1000026527"
FT ACT_SITE 143
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ SEQUENCE 373 AA; 40721 MW; 8CBA28D2654CF1FA CRC64;
MTAQNPNLAA LSAAGVSVWL DDLSRDRLRS GNLQELIDTK SVVGVTTNPS IFQKALSEGH
TYDAQIAELA ARGADVDATI RTVTTDDVRS ACDVLVPQWE DSDGVDGRVS IEVDPRLAHE
TEKTIQQAIE LWKIVDRPNL FIKIPATKAG LPAISAVLAE GISVNVTLIF SVQRYREVMD
AYLTGMEKAR QAGHSLSKIH SVASFFVSRV DTEIDKRLDR IGSRQALELR GQAGVANARL
AYATYREVFE DSDRYRSLKV DGARVQRPLW ASTGVKNPDY SDTLYVTELV APHTVNTMPE
KTIDAVADHG VIQGDTVTGT ASDAQAVFDQ LGAIGIDLTD VFAVLEEEGV RKFEASWNEL
LQETRAHLDT AAQ