ID TAL_BACTN Reviewed; 218 AA.
AC Q8A767;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 71.
DE RecName: Full=Probable transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=BT_1658;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS 10582 / E50 / VPI-5482).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA Chiang H.C., Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Transaldolase is important for the balance of
CC metabolites in the pentose-phosphate pathway (By similarity).
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
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
CC stage): step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B
CC subfamily.
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DR EMBL; AE015928; AAO76765.1; -; Genomic_DNA.
DR RefSeq; NP_810571.1; NC_004663.1.
DR ProteinModelPortal; Q8A767; -.
DR STRING; 226186.BT_1658; -.
DR EnsemblBacteria; AAO76765; AAO76765; BT_1658.
DR GeneID; 1075635; -.
DR KEGG; bth:BT_1658; -.
DR PATRIC; 21058206; VBIBacThe70966_1699.
DR eggNOG; COG0176; -.
DR HOGENOM; HOG000226073; -.
DR KO; K00616; -.
DR OMA; DNYGFET; -.
DR ProtClustDB; PRK01362; -.
DR BioCyc; BTHE226186:GJXV-1690-MONOMER; -.
DR UniPathway; UPA00115; UER00414.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:HAMAP.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; Transaldolase.
DR InterPro; IPR004731; Transaldolase_3A/3B.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; Transaldolase; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Pentose shunt; Reference proteome;
KW Transferase.
FT CHAIN 1 218 Probable transaldolase.
FT /FTId=PRO_0000173659.
FT ACT_SITE 87 87 By similarity.
SQ SEQUENCE 218 AA; 23775 MW; 3FC4F3516694DA94 CRC64;
MKFFIDTANL EQIQEAYDLG VLDGVTTNPS LMAKEGIKGT ENQREHYIKI CKIVNADVSA
EVIATDYEGM IREGEELAAL NPHIVVKVPC IADGIKAIKY FTEKGIRTNC TLVFSVGQAL
LAAKAGATYV SPFVGRLDDI CEDGVGLVGD IVRMYRTYDY KTQVLAASIR NTKHIIECVE
VGADVATCPL SAIKGLLNHP LTDSGLKKFL EDYKKVNG
//
