(data stored in SCRATCH zone)

SWISSPROT: B7UI53_ECO27

ID   B7UI53_ECO27            Unreviewed;       317 AA.
AC   B7UI53;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00492, ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS00118670};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00492, ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS00118670};
GN   Name=talB {ECO:0000313|EMBL:CAS07556.1};
GN   Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=E2348C_0008 {ECO:0000313|EMBL:CAS07556.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07556.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07556.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000256|HAMAP-
CC       Rule:MF_00492, ECO:0000256|RuleBase:RU004155,
CC       ECO:0000256|SAAS:SAAS00768481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-
CC         phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC         EC=2.2.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00492,
CC         ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS01126537};
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:0000256|HAMAP-Rule:MF_00492,
CC       ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS00118684}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS00768512}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492,
CC       ECO:0000256|SAAS:SAAS00768485}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00492, ECO:0000256|RuleBase:RU004155,
CC       ECO:0000256|SAAS:SAAS00736059}.
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DR   EMBL; FM180568; CAS07556.1; -; Genomic_DNA.
DR   RefSeq; WP_000130187.1; NC_011601.1.
DR   SMR; B7UI53; -.
DR   EnsemblBacteria; CAS07556; CAS07556; E2348C_0008.
DR   KEGG; ecg:E2348C_0008; -.
DR   HOGENOM; HOG000281234; -.
DR   KO; K00616; -.
DR   OMA; ILDWFKA; -.
DR   BioCyc; ECOL574521:E2348C_RS00045-MONOMER; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase 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; 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   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; B7UI53.
DR   SWISS-2DPAGE; B7UI53.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492,
KW   ECO:0000256|SAAS:SAAS00768492};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00492,
KW   ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS00118654};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00492,
KW   ECO:0000256|SAAS:SAAS00118695};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00492,
KW   ECO:0000256|RuleBase:RU004155, ECO:0000256|SAAS:SAAS00118651}.
FT   ACT_SITE    132    132       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00492}.
SQ   SEQUENCE   317 AA;  35205 MW;  2DF03D741E4FCF31 CRC64;
     MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK
     QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN
     DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
     RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD
     RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
     KFAVDQEKLE KMIGDLL
//

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