TAL_THEAC
ID TAL_THEAC Reviewed; 223 AA.
AC Q9HKI3;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Probable transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=Ta0616;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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 3B subfamily.
CC {ECO:0000305}.
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DR EMBL; AL445064; CAC11755.1; -; Genomic_DNA.
DR RefSeq; WP_010901039.1; NC_002578.1.
DR PDB; 3S0C; X-ray; 1.78 A; A/B/C/D/E=1-223.
DR PDB; 3S1U; X-ray; 1.90 A; A/B/C/D/E=1-223.
DR PDB; 3S1V; X-ray; 1.80 A; A/B/C/D/E=1-223.
DR PDB; 3S1W; X-ray; 1.80 A; A/B/C/D/E=1-223.
DR PDB; 3S1X; X-ray; 1.65 A; A/B/C/D/E=1-223.
DR PDB; 4XZ9; X-ray; 1.80 A; A/B/C/D/E=1-223.
DR PDB; 6YR3; X-ray; 1.48 A; A/B/C/D/E=1-223.
DR PDB; 6YRE; X-ray; 1.96 A; A/B/C/D/E=1-223.
DR PDB; 6YRH; X-ray; 1.80 A; A/B/C/D/E=1-223.
DR PDB; 6YRM; X-ray; 1.70 A; A/B/C/D/E=1-223.
DR PDB; 6YRT; X-ray; 1.65 A; A/B/C/D/E=1-223.
DR PDB; 6YS0; X-ray; 1.70 A; A/B/C/D/E=1-223.
DR PDBsum; 3S0C; -.
DR PDBsum; 3S1U; -.
DR PDBsum; 3S1V; -.
DR PDBsum; 3S1W; -.
DR PDBsum; 3S1X; -.
DR PDBsum; 4XZ9; -.
DR PDBsum; 6YR3; -.
DR PDBsum; 6YRE; -.
DR PDBsum; 6YRH; -.
DR PDBsum; 6YRM; -.
DR PDBsum; 6YRT; -.
DR PDBsum; 6YS0; -.
DR AlphaFoldDB; Q9HKI3; -.
DR SMR; Q9HKI3; -.
DR STRING; 273075.Ta0616; -.
DR EnsemblBacteria; CAC11755; CAC11755; CAC11755.
DR GeneID; 1456197; -.
DR KEGG; tac:Ta0616; -.
DR eggNOG; arCOG05061; Archaea.
DR HOGENOM; CLU_079764_0_0_2; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 77186at2157; -.
DR BRENDA; 2.2.1.2; 6324.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; Q9HKI3; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pentose shunt; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1..223
FT /note="Probable transaldolase"
FT /id="PRO_0000173691"
FT ACT_SITE 86
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:6YR3"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:6YR3"
FT HELIX 199..215
FT /evidence="ECO:0007829|PDB:6YR3"
SQ SEQUENCE 223 AA; 24437 MW; A81C5F74B856E736 CRC64;
MKIFLDTANI DEIRTGVNWG IVDGVTTNPT LISKEAVNGK KYGDIIREIL KIVDGPVSVE
VVSTKYEGMV EEARKIHGLG DNAVVKIPMT EDGLRAIKTL SSEHINTNCT LVFNPIQALL
AAKAGATYVS PFVGRLDDIG EDGMQIIDMI RTIFNNYIIK TQILVASIRN PIHVLRSAVI
GADVVTVPFN VLKSLMKHPK TDEGLAKFLE DWKKVSPDGK LIL
