Q59288 · CSLA_PEDHD
- ProteinChondroitinase-AC
- GenecslA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids700 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 225 | |||||
Sequence: H | ||||||
Active site | 234 | |||||
Sequence: Y | ||||||
Active site | 288 | |||||
Sequence: R | ||||||
Binding site | 405 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 407 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 416 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 417 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | carbohydrate binding | |
Molecular Function | chondroitin AC lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChondroitinase-AC
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter
Accessions
- Primary accessionQ59288
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MKKLFVTCIVFFSILSPALLIA | ||||||
Chain | PRO_0000024927 | 23-700 | Chondroitinase-AC | |||
Sequence: QQTGTAELIMKRVMLDLKKPLRNMDKVAEKNLNTLQPDGSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVFDQISKAFKYWYDSDPKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIALHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFITGVLKLANYVRDTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKAEKKRLLVAKMIDLKHTEEWADAIARTDSTVAAGYKIEPYHHQFWNGDYVQHLRPAYSFNVRMVSKRTRRSESGNKENLLGRYLSDGATNIQLRGPEYYNIMPVWEWDKIPGITSRDYLTDRPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDSLQAKKAWFFFDKEIVCLGAGINSNAPENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQSQKGNWFHINNSHSKDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAPKVLANTNQLQAVYHQQLDMVQAIFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAADPLQKEKTAVLSIRDLKTGKTNRVKIDFPQQEFAGATVELK | ||||||
Glycosylation | 328 | O-linked (Man...) serine | ||||
Sequence: S | ||||||
Glycosylation | 455 | O-linked (Man...) serine | ||||
Sequence: S |
Keywords
- PTM
PTM databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length700
- Mass (Da)79,694
- Last updated1996-11-01 v1
- ChecksumC36B608FCAFFC656
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U27583 EMBL· GenBank· DDBJ | AAC83383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001681 EMBL· GenBank· DDBJ | ACU03008.1 EMBL· GenBank· DDBJ | Genomic DNA |