ID   A5FID4_FLAJ1            Unreviewed;       218 AA.
AC   A5FID4;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   04-NOV-2026, entry version 118.
DE   RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00494};
GN   OrderedLocusNames=Fjoh_2002 {ECO:0000313|EMBL:ABQ05034.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC
OS   14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga
OS   johnsonae).
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05034.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ05034.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 /
RC   NBRC 14942 / NCIMB 11054 / UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
CC   -!- FUNCTION: Transaldolase involved in the non-oxidative phase in the
CC       pentose phosphate pathway. Catalyzes the reversible conversion of
CC       sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is
CC       important for the balance of metabolites in the pentose-phosphate
CC       pathway. {ECO:0000256|HAMAP-Rule:MF_00494}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate =
CC         D-erythrose 4-phosphate + beta-D-fructose 6-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:0000256|HAMAP-Rule:MF_00494};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate = dihydroxyacetone + D-
CC         glyceraldehyde 3-phosphate; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC         Evidence={ECO:0000256|ARBA:ARBA00048809};
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:0000256|HAMAP-Rule:MF_00494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00494}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005740, ECO:0000256|HAMAP-Rule:MF_00494}.
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DR   EMBL; CP000685; ABQ05034.1; -; Genomic_DNA.
DR   RefSeq; WP_012024074.1; NC_009441.1.
DR   AlphaFoldDB; A5FID4; -.
DR   STRING; 376686.Fjoh_2002; -.
DR   GeneID; 31764904; -.
DR   KEGG; fjo:Fjoh_2002; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_10; -.
DR   OrthoDB; 9807051at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0042182; P:ketone catabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00956; Transaldolase_FSA; 1.
DR   FunFam; 3.20.20.70:FF:000018; Probable transaldolase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR00875; fsa_talC_mipB; 1.
DR   PANTHER; PTHR10683:SF40; FRUCTOSE-6-PHOSPHATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00494};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW   Rule:MF_00494}; Reference proteome {ECO:0000313|Proteomes:UP000006694};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00494}.
FT   ACT_SITE        61
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   ACT_SITE        87
FT                   /note="Nucleophile; Schiff-base intermediate with
FT                   substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         6
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         28
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         87
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         109
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         131
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         136
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         168
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
FT   BINDING         170
FT                   /ligand="D-fructose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61527"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   218 AA;  23659 MW;  2E1B9CD95DC46673 CRC64;
     MKFFIDTANL QDIEEAQALG VLDGVTTNPS LMAKEGITGK ENILKHYLDI CNIVDGDVSA
     EVISTDFEGM VREGEELAAL HPQIVVKLPM IGDGVKACKY FSSKGIKTNV TLVFSAGQAL
     LAAKAGATYV SPFLGRLDDV STDGMHLIEE IREIYDNYNY QTQILSASVR HTMHIVNCAK
     VGSDVMTGPL SAIKGLLKHP LTDIGLKQFV EDAKKMNL
//