| IED ID | IndEnz0001000335 |
| Enzyme Type ID | amylase000335 |
| Protein Name |
Sucrose phosphorylase SP SPase EC 2.4.1.7 |
| Gene Name | sucP spl BAD_0078 |
| Organism | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Bifidobacteriales Bifidobacteriaceae Bifidobacterium Bifidobacterium adolescentis Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
| Enzyme Sequence | MKNKVQLITYADRLGDGTIKSMTDILRTRFDGVYDGVHILPFFTPFDGADAGFDPIDHTKVDERLGSWDDVAELSKTHNIMVDAIVNHMSWESKQFQDVLAKGEESEYYPMFLTMSSVFPNGATEEDLAGIYRPRPGLPFTHYKFAGKTRLVWVSFTPQQVDIDTDSDKGWEYLMSIFDQMAASHVSYIRLDAVGYGAKEAGTSCFMTPKTFKLISRLREEGVKRGLEILIEVHSYYKKQVEIASKVDRVYDFALPPLLLHALSTGHVEPVAHWTDIRPNNAVTVLDTHDGIGVIDIGSDQLDRSLKGLVPDEDVDNLVNTIHANTHGESQAATGAAASNLDLYQVNSTYYSALGCNDQHYIAARAVQFFLPGVPQVYYVGALAGKNDMELLRKTNNGRDINRHYYSTAEIDENLKRPVVKALNALAKFRNELDAFDGTFSYTTDDDTSISFTWRGETSQATLTFEPKRGLGVDNTTPVAMLEWEDSAGDHRSDDLIANPPVVA |
| Enzyme Length | 504 |
| Uniprot Accession Number | A0ZZH6 |
| Absorption | |
| Active Site | ACT_SITE 192; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:16990265, ECO:0000305|PubMed:14756551"; ACT_SITE 232; /note="Proton donor"; /evidence="ECO:0000305|PubMed:14756551, ECO:0000305|PubMed:16990265" |
| Activity Regulation | |
| Binding Site | BINDING 50; /note="Substrate"; /evidence="ECO:0000269|PubMed:16990265, ECO:0007744|PDB:2GDU"; BINDING 88; /note="Sucrose"; /evidence="ECO:0000269|PubMed:16990265, ECO:0007744|PDB:2GDU"; BINDING 232; /note="Sucrose"; /evidence="ECO:0000269|PubMed:16990265, ECO:0007744|PDB:2GDU"; BINDING 399; /note="Sucrose"; /evidence="ECO:0000269|PubMed:16990265, ECO:0007744|PDB:2GDU" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=phosphate + sucrose = alpha-D-glucose 1-phosphate + D-fructose; Xref=Rhea:RHEA:24048, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.7; Evidence={ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225}; |
| DNA Binding | |
| EC Number | 2.4.1.7 |
| Enzyme Function | FUNCTION: Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189). {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius for the phosphorolysis of sucrose (PubMed:14740189). The His-tagged enzyme shows an optimum temperature of 58 degrees Celsius (PubMed:20691225). The immobilization of the enzyme on Sepabeads EC-HFA increases thermostability, and optimum temperature is shifted to 65 degrees Celsius (PubMed:20691225). {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5 for the phosphorolysis of sucrose. {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (25); Binding site (4); Chain (1); Helix (26); Mutagenesis (2); Region (3); Turn (7) |
| Keywords | 3D-structure;Carbohydrate metabolism;Direct protein sequencing;Glycosyltransferase;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 1R7A; 2GDU; 2GDV; 5C8B; 5M9X; 5MAN; 5MB2; 6FME; |
| Mapped Pubmed ID | 29057405; |
| Motif | |
| Gene Encoded By | |
| Mass | 56,190 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.8 mM for sucrose (at 58 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:20691225}; Note=kcat is 207 sec(-1) for the phosphorolysis of sucrose (at 58 degrees Celsius and pH 6.5). {ECO:0000269|PubMed:20691225}; |
| Metal Binding | |
| Rhea ID | RHEA:24048 |
| Cross Reference Brenda | 2.4.1.7; |