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TAL_CERSK
ID   TAL_CERSK               Reviewed;         219 AA.
AC   B9KKW2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Probable transaldolase {ECO:0000255|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00494}; OrderedLocusNames=RSKD131_1899;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00494}.
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:0000255|HAMAP-Rule:MF_00494};
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. {ECO:0000255|HAMAP-Rule:MF_00494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00494}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00494}.
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DR   EMBL; CP001150; ACM01759.1; -; Genomic_DNA.
DR   RefSeq; WP_002720727.1; NC_011963.1.
DR   AlphaFoldDB; B9KKW2; -.
DR   SMR; B9KKW2; -.
DR   EnsemblBacteria; ACM01759; ACM01759; RSKD131_1899.
DR   GeneID; 57470883; -.
DR   GeneID; 67447295; -.
DR   KEGG; rsk:RSKD131_1899; -.
DR   HOGENOM; CLU_079764_0_0_5; -.
DR   OMA; VRHPMHV; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001597; Chromosome 1.
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   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT   CHAIN           1..219
FT                   /note="Probable transaldolase"
FT                   /id="PRO_1000198476"
FT   ACT_SITE        83
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   219 AA;  23391 MW;  DF54E13E53ED17DE CRC64;
     MKFFVDSADV AAIAELNALG MVDGVTTNPS LILKSGRNIL EVTKEICNLV SGPVSAEVVA
     AKAEDMIEEG RHLAEIAPNI AVKVPLTWDG LRACKVLSDE GRMVNVTLCF SVNQALLAAK
     AGATFISPFI GRLDDINLDG MELIADIRQV YDNYDFKTEV LAASVRTPNH VADCARIGAD
     VITAPPAVIK ALANHVLTDK GLDMFNADWA KTGQSILLK
 
 
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