Q9F8X1 · CHBP_VIBFU

  • Protein
    N,N'-diacetylchitobiose phosphorylase
  • Gene
    chbP
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

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

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.58 mMN,N'-diacetylchitobiose
0.51 mMphosphate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
4.6 nmol/min/ugwith N,N'-diacetylchitobiose as substrate
4.8 nmol/min/ugwith 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.

TypeIDPosition(s)Description
Binding site333N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site343N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site349N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site350N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site490N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Active site492Proton donor
Binding site492N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site492N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site636N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site637N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site637N-acetyl-D-glucosamine (UniProtKB | ChEBI)
Binding site644N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site690N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site709N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)
Binding site710N-acetyl-alpha-D-glucosamine 1-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functioncarbohydrate binding
Molecular Functionglycosyltransferase activity
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    N,N'-diacetylchitobiose phosphorylase
  • EC number
  • Alternative names
    • Chitobiose phosphorylase

Gene names

    • Name
      chbP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio

Accessions

  • Primary accession
    Q9F8X1

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004241081-800N,N'-diacetylchitobiose phosphorylase

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 94 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    800
  • Mass (Da)
    89,667
  • Last updated
    2001-03-01 v1
  • Checksum
    6775D823C051122A
MKYGYFDNDNREYVITRPDVPAPWTNYLGTEKFCTVISHNAGGYSFYHSPEYNRVTKFRPNFTQDRPGHYIYLRDDETGDFWSVSWQPVAKNLDDAHYEVRHGLSYSKFRCDYNGIVATKTLFVPKGEDAQVWDVEIENTSDQPRTISAFGYVEFSFSHIASDNQNHQMSLYSAGTEYNNGVLEYDLYYNTDDFLGFYYLTATFDADSYDGQRDAFLGMYRDEANPIAVANGRCSNSAQTCYNHCGALHKQFVLQPGEKVRFAVILGVGKGNGEKLRAKYQDLSQVDAAFAGIKQHWDERCAKFQVRSPNQGLDTMINAWTLYQAETCVVWSRFASFIEVGGRTGLGYRDTAQDAISVPHTNPAMTRKRLVDLLRGQVKAGYGLHLFDPDWFDPEKADVKPSKSPTVVPTPSDEDKIHGIKDTCSDDHLWIVPTILNFVKETGDLSFIDEVIPYADGGDATVYQHMMAALDFSAEYVGQTGICKGLRADWNDCLNLGGGESAMVSFLHFWALEAFLELARHRQDAAAIDKYQAMANGVREACETHLWDDNGGWYIRGLTKDGDKIGTFEQQEGKVHLESNTLAVLSGAVSQQRGEKAMDAVYEYLFSPYGLHLNAPSFATPNDDIGFVTRVYQGVKENGAIFSHPNPWAWVAEAKLGRGDRAMEFYDSLNPYNQNDIIETRVAEPYSYVQFIMGRDHQDHGRANHPWLTGTSGWAYYATTNFILGVRTGFDTLTVDPCIPAAWSGFEVTREWRGATYHISVQNPNGVSKGVQSILVNGEAVDAINAQPAGSENQVTVILG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF230379
EMBL· GenBank· DDBJ
AAG23740.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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