(data stored in ACNUC7421 zone)

SWISSPROT: TAL_EDWI9

ID   TAL_EDWI9               Reviewed;         317 AA.
AC   C5B7L0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=NT01EI_0665;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_00492}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00492}.
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. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00492}.
DR   EMBL; CP001600; ACR67887.1; -; Genomic_DNA.
DR   RefSeq; WP_015870081.1; NC_012779.2.
DR   SMR; C5B7L0; -.
DR   STRING; 634503.NT01EI_0665; -.
DR   PRIDE; C5B7L0; -.
DR   EnsemblBacteria; ACR67887; ACR67887; NT01EI_0665.
DR   GeneID; 7961999; -.
DR   KEGG; eic:NT01EI_0665; -.
DR   PATRIC; fig|634503.3.peg.599; -.
DR   eggNOG; ENOG4105CW3; Bacteria.
DR   eggNOG; COG0176; LUCA.
DR   HOGENOM; HOG000281234; -.
DR   KO; K00616; -.
DR   OMA; MAFDKLH; -.
DR   OrthoDB; POG091H05RO; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF22; PTHR10683:SF22; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7L0.
DR   SWISS-2DPAGE; C5B7L0.
KW   Complete proteome; Cytoplasm; Pentose shunt; Reference proteome;
KW   Schiff base; Transferase.
FT   CHAIN         1    317       Transaldolase.
FT                                /FTId=PRO_1000206463.
FT   ACT_SITE    132    132       Schiff-base intermediate with substrate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00492}.
SQ   SEQUENCE   317 AA;  34843 MW;  04B5850B7BED5367 CRC64;
     MTDKLTSLRQ LTTVVADTGD IAAMKQYQPQ DATTNPSLIL NAAQIPEYRK LIDDAIAWAR
     AQSGDRAQQI VDASDKLAVN IGLEILKLIP GRISTEVDAR LSYDTEASVA KAKRLIKLYN
     DAGISNDRIL IKLASTWQGI RAAERLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
     RILDWHKANG GKSEFAPAED PGVISVTEIY NYYKQHGYET VVMGASFRNV GEILELAGCD
     RLTISPPLLK ELSESTGNVE RKLADQGEIK ARPARMSEAE FYWQHNQDPM AVEKLADGIR
     KFAVDQGKLE SMIGALL
//

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