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Database: UniProt
Entry: H8KUC0_SOLCM
LinkDB: H8KUC0_SOLCM
Original site: H8KUC0_SOLCM 
ID   H8KUC0_SOLCM            Unreviewed;       221 AA.
AC   H8KUC0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=Probable 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=Solca_2243 {ECO:0000313|EMBL:AFD07285.1};
OS   Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS   12057 / USAM 9D) (Flexibacter canadensis).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Solitalea.
OX   NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD07285.1, ECO:0000313|Proteomes:UP000007590};
RN   [1] {ECO:0000313|Proteomes:UP000007590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC   {ECO:0000313|Proteomes:UP000007590};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Solitalea canadensis DSM 3403.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|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:0000256|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC       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; CP003349; AFD07285.1; -; Genomic_DNA.
DR   RefSeq; WP_014680512.1; NC_017770.1.
DR   AlphaFoldDB; H8KUC0; -.
DR   STRING; 929556.Solca_2243; -.
DR   KEGG; scn:Solca_2243; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_10; -.
DR   OrthoDB; 9807051at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000007590; 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; 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:UP000007590};
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        87
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   221 AA;  23652 MW;  3BA46016088F99AF CRC64;
     MKFFIDTANL AQIKEAQDLG VLDGVTTNPS LMAKEGITGD DNVLAHYKAI CDLVDDNVSA
     EVISTDFEGM IAEGERLAAI DKKIVVKVPM IADGVKALKY FSKKGIRTNC TLVFSAGQAL
     LAAKAGASYV SPFVGRLDDI STDGLQLIED IRLIYDNYGY ETEILAASVR HPMHIIECAK
     IGADVMTGPL SAIKALLKHP LTDIGLQQFL ADHAKAAAAT K
//
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