(data stored in SCRATCH zone)

SWISSPROT: C8U184_ECO10

ID   C8U184_ECO10            Unreviewed;       317 AA.
AC   C8U184;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
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:BAI28892.1};
GN   Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN   OrderedLocusNames=ECO103_0009 {ECO:0000313|EMBL:BAI28892.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28892.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28892.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI28892.1; -; Genomic_DNA.
DR   RefSeq; WP_000130185.1; NC_013353.1.
DR   SMR; C8U184; -.
DR   EnsemblBacteria; BAI28892; BAI28892; ECO103_0009.
DR   KEGG; eoh:ECO103_0009; -.
DR   HOGENOM; HOG000281234; -.
DR   KO; K00616; -.
DR   OMA; ILDWFKA; -.
DR   BioCyc; ECOL585395:ECO103_RS00050-MONOMER; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000959; 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; C8U184.
DR   SWISS-2DPAGE; C8U184.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  35219 MW;  2DF03D741E576C31 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
     KFAIDQEKLE KMIGDLL
//

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