ID   TAL_JANSC               Reviewed;         217 AA.
AC   Q28TL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Jann_1032;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000264; ABD53949.1; -; Genomic_DNA.
DR   RefSeq; WP_011454156.1; NC_007802.1.
DR   AlphaFoldDB; Q28TL3; -.
DR   SMR; Q28TL3; -.
DR   STRING; 290400.Jann_1032; -.
DR   EnsemblBacteria; ABD53949; ABD53949; Jann_1032.
DR   KEGG; jan:Jann_1032; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_5; -.
DR   OMA; VRHPMHV; -.
DR   OrthoDB; 784333at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000008326; Chromosome.
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; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..217
FT                   /note="Probable transaldolase"
FT                   /id="PRO_1000126323"
FT   ACT_SITE        83
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   217 AA;  23103 MW;  8EA6CABA741D7CAA CRC64;
     MKFFVDTADI DAIRELHELG MVDGVTTNPS LIMKSGRDIK EVTAEICALV DGPVSAETVA
     LDADGMINEG RELAKIADNI TIKVPLTWAG LQACKVLSGE GRMVNVTLCF SANQALLAAK
     AGATFISPFV GRLDDLNMDG MDLIAEIRQI YDNYGFETEI LVASIRSANH MKDAALIGAD
     VATAPPGVIK AMANHVMTDK GLDAFMADWA KTGQSIV