Q9F8X1 · CHBP_VIBFU
- ProteinN,N'-diacetylchitobiose phosphorylase
- GenechbP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids800 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Catalyzes the reversible phosphorolysis of chitobiose (N,N'-diacetylchitobiose or (GlcNAc)2) into N-acetyl-alpha-D-glucosamine 1-phosphate (GlcNAc-1-P) and N-acetyl-D-glucosamine (GlcNAc) with inversion of the anomeric configuration.
Catalytic activity
- N,N'-diacetylchitobiose + phosphate = N-acetyl-alpha-D-glucosamine 1-phosphate + N-acetyl-D-glucosamine
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.58 mM | N,N'-diacetylchitobiose | |||||
0.51 mM | phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
4.6 nmol/min/ug | with N,N'-diacetylchitobiose as substrate | ||||
4.8 nmol/min/ug | with phosphate as substrate |
pH Dependence
Optimum pH is 6.5-7.0.
Temperature Dependence
Optimum temperature is 20-37 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 333 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 343 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 349 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 350 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 490 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Active site | 492 | Proton donor | ||||
Sequence: D | ||||||
Binding site | 492 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 492 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 636 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 637 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 637 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 644 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 690 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 709 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 710 | N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carbohydrate binding | |
Molecular Function | glycosyltransferase activity | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameN,N'-diacetylchitobiose phosphorylase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionQ9F8X1
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000424108 | 1-800 | N,N'-diacetylchitobiose phosphorylase | |||
Sequence: MKYGYFDNDNREYVITRPDVPAPWTNYLGTEKFCTVISHNAGGYSFYHSPEYNRVTKFRPNFTQDRPGHYIYLRDDETGDFWSVSWQPVAKNLDDAHYEVRHGLSYSKFRCDYNGIVATKTLFVPKGEDAQVWDVEIENTSDQPRTISAFGYVEFSFSHIASDNQNHQMSLYSAGTEYNNGVLEYDLYYNTDDFLGFYYLTATFDADSYDGQRDAFLGMYRDEANPIAVANGRCSNSAQTCYNHCGALHKQFVLQPGEKVRFAVILGVGKGNGEKLRAKYQDLSQVDAAFAGIKQHWDERCAKFQVRSPNQGLDTMINAWTLYQAETCVVWSRFASFIEVGGRTGLGYRDTAQDAISVPHTNPAMTRKRLVDLLRGQVKAGYGLHLFDPDWFDPEKADVKPSKSPTVVPTPSDEDKIHGIKDTCSDDHLWIVPTILNFVKETGDLSFIDEVIPYADGGDATVYQHMMAALDFSAEYVGQTGICKGLRADWNDCLNLGGGESAMVSFLHFWALEAFLELARHRQDAAAIDKYQAMANGVREACETHLWDDNGGWYIRGLTKDGDKIGTFEQQEGKVHLESNTLAVLSGAVSQQRGEKAMDAVYEYLFSPYGLHLNAPSFATPNDDIGFVTRVYQGVKENGAIFSHPNPWAWVAEAKLGRGDRAMEFYDSLNPYNQNDIIETRVAEPYSYVQFIMGRDHQDHGRANHPWLTGTSGWAYYATTNFILGVRTGFDTLTVDPCIPAAWSGFEVTREWRGATYHISVQNPNGVSKGVQSILVNGEAVDAINAQPAGSENQVTVILG |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length800
- Mass (Da)89,667
- Last updated2001-03-01 v1
- Checksum6775D823C051122A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF230379 EMBL· GenBank· DDBJ | AAG23740.1 EMBL· GenBank· DDBJ | Genomic DNA |