TAL_THEMA
ID TAL_THEMA Reviewed; 218 AA.
AC Q9WYD1;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=TM_0295;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11120740; DOI=10.1074/jbc.m008061200;
RA Schuermann M., Sprenger G.A.;
RT "Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia
RT coli and is related to a novel group of bacterial transaldolases.";
RL J. Biol. Chem. 276:11055-11061(2001).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. Does not show fructose-6-P aldolase
CC activity. {ECO:0000269|PubMed:11120740}.
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:0000269|PubMed:11120740};
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:0000305}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35383.1; -; Genomic_DNA.
DR PIR; G72394; G72394.
DR RefSeq; NP_228107.1; NC_000853.1.
DR RefSeq; WP_004083013.1; NZ_CP011107.1.
DR PDB; 1VPX; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-218.
DR PDBsum; 1VPX; -.
DR AlphaFoldDB; Q9WYD1; -.
DR SMR; Q9WYD1; -.
DR STRING; 243274.THEMA_03250; -.
DR EnsemblBacteria; AAD35383; AAD35383; TM_0295.
DR KEGG; tma:TM0295; -.
DR eggNOG; COG0176; Bacteria.
DR InParanoid; Q9WYD1; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 784333at2; -.
DR BRENDA; 2.2.1.2; 6331.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; Q9WYD1; -.
DR Proteomes; UP000008183; 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..218
FT /note="Transaldolase"
FT /id="PRO_0000173687"
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 140..154
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:1VPX"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:1VPX"
FT HELIX 196..214
FT /evidence="ECO:0007829|PDB:1VPX"
SQ SEQUENCE 218 AA; 24213 MW; 3FF8B0A85CFA6EFA CRC64;
MKIFLDTANL EEIKKGVEWG IVDGVTTNPT LISKEGAEFK QRVKEICDLV KGPVSAEVVS
LDYEGMVREA RELAQISEYV VIKIPMTPDG IKAVKTLSAE GIKTNVTLVF SPAQAILAAK
AGATYVSPFV GRMDDLSNDG MRMLGEIVEI YNNYGFETEI IAASIRHPMH VVEAALMGVD
IVTMPFAVLE KLFKHPMTDL GIERFMEDWK KYLENLKK
