| IED ID | IndEnz0001000346 |
| Enzyme Type ID | amylase000346 |
| Protein Name |
Sucrose 6 F -phosphate phosphorylase EC 2.4.1.329 Sucrose 6'-phosphate phosphorylase SPP |
| Gene Name | spp Tthe_1921 |
| Organism | Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Thermoanaerobacterium Thermoanaerobacterium thermosaccharolyticum (Clostridium thermosaccharolyticum) Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium thermosaccharolyticum) |
| Enzyme Sequence | MALKNKVQLITYPDSLGGNLKTLNDVLEKYFSDVFGGVHILPPFPSSGDRGFAPITYSEIEPKFGTWYDIKKMAENFDILLDLMVNHVSRRSIYFQDFLKKGRKSEYADMFITLDKLWKDGKPVKGDIEKMFLRRTLPYSTFKIEETGEEEKVWTTFGKTDPSEQIDLDVNSHLVREFLLEVFKTFSNFGVKIVRLDAVGYVIKKIGTSCFFVEPEIYEFLDWAKGQAASYGIELLLEVHSQFEVQYKLAERGFLIYDFILPFTVLYTLINKSNEMLYHYLKNRPINQFTMLDCHDGIPVKPDLDGLIDTKKAKEVVDICVQRGANLSLIYGDKYKSEDGFDVHQINCTYYSALNCDDDAYLAARAIQFFTPGIPQVYYVGLLAGVNDFEAVKKTKEGREINRHNYGLKEIEESVQKNVVQRLLKLIRFRNEYEAFNGEFFIEDCRKDEIRLTWKKDDKRCSLFIDLKTYKTTIDYINENGEEVKYLV |
| Enzyme Length | 488 |
| Uniprot Accession Number | D9TT09 |
| Absorption | |
| Active Site | ACT_SITE 197; /note=Nucleophile; /evidence=ECO:0000305|PubMed:31405215; ACT_SITE 238; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:31405215 |
| Activity Regulation | |
| Binding Site | BINDING 49; /note=Sucrose 6(F)-phosphate; /evidence=ECO:0000250|UniProtKB:A0ZZH6; BINDING 87; /note=Sucrose 6(F)-phosphate; /evidence=ECO:0000250|UniProtKB:A0ZZH6; BINDING 238; /note=Sucrose 6(F)-phosphate; /evidence=ECO:0000250|UniProtKB:A0ZZH6; BINDING 399; /note=Sucrose 6(F)-phosphate; /evidence=ECO:0000250|UniProtKB:A0ZZH6 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=phosphate + sucrose 6(F)-phosphate = alpha-D-glucose 1-phosphate + beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:38863, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723, ChEBI:CHEBI:58601; EC=2.4.1.329; Evidence={ECO:0000269|PubMed:24599311};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38864; Evidence={ECO:0000305|PubMed:24599311}; |
| DNA Binding | |
| EC Number | 2.4.1.329 |
| Enzyme Function | FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)-phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-phosphate. May be involved in a new pathway for the degradation of sucrose, which could become phosphorylated on its fructose moiety during uptake via a PTS system. To a lesser extent, can also reversibly act on sucrose in vitro (PubMed:24599311). Is also able to catalyze transglycosylation reactions in vitro (PubMed:26074151). {ECO:0000269|PubMed:24599311, ECO:0000269|PubMed:26074151}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:24599311}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 and 6.5 for the synthetic and phosphorolytic reaction, respectively. Thermostable. Has a half-life of 60 hours at 60 degrees Celsius. {ECO:0000269|PubMed:24599311}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (24); Binding site (4); Chain (1); Helix (24); Mutagenesis (4); Region (3); Site (1); Turn (6) |
| Keywords | 3D-structure;Carbohydrate metabolism;Glycosyltransferase;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6S9V; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,716 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 mM for phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=12.7 mM for sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=76.5 mM for sucrose (at 55 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:24599311}; KM=15.1 mM for D-fructose 6-phosphate (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; KM=15.6 mM for alpha-D-glucose 1-phosphate (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; KM=41.6 mM for D-fructose (at 55 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:24599311}; Note=kcat is 82.6 sec(-1) for the phosphorolysis of sucrose 6(F)-phosphate (at 55 degrees Celsius and pH 6.5). kcat is 66.2 sec(-1) for the phosphorolysis of sucrose (at 55 degrees Celsius and pH 6.5). kcat is 24.2 sec(-1) for the synthetic direction with alpha-D-glucose 1-phosphate and D-fructose 6-phosphate as substrates (at 55 degrees Celsius and pH 6.0). kcat is 14.4 sec(-1) for the synthetic direction with alpha-D-glucose 1-phosphate and D-fructose as substrates (at 55 degrees Celsius and pH 6.0). {ECO:0000269|PubMed:24599311}; |
| Metal Binding | |
| Rhea ID | RHEA:38863; RHEA:38864 |
| Cross Reference Brenda | 2.4.1.329; |