Q8A2I1 · CABC2_BACTN
- ProteinChondroitin sulfate ABC exolyase
- Genechonabc
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1014 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against acharan sulfate, heparin or heparan sulfate.
Catalytic activity
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Note: Divalent metal cation. Requires divalent metal cation for binding of dermatan sulfate substrate, whereas it is not necessary for the binding of chondroitin sulfate substrates. Prefers Ca2+ or Mg2+, binding 1 ion per subunit.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 24 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 26 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 50 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 53 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 161 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 172 | Important for catalytic activity against all substrates | ||||
Sequence: R | ||||||
Site | 344 | Important for catalytic activity against dermatan sulfate substrate | ||||
Sequence: H | ||||||
Active site | 345 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 454 | Proton acceptor | ||||
Sequence: H | ||||||
Active site | 461 | Proton donor | ||||
Sequence: Y | ||||||
Site | 514 | Transition state stabilizer | ||||
Sequence: R | ||||||
Site | 628 | Important for catalytic activity against all substrates | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | periplasmic space | |
Molecular Function | carbohydrate binding | |
Molecular Function | carbon-oxygen lyase activity, acting on polysaccharides | |
Molecular Function | chondroitin AC lyase activity | |
Molecular Function | chondroitin B lyase activity | |
Molecular Function | chondroitin-sulfate-ABC endolyase activity | |
Molecular Function | chondroitin-sulfate-ABC exolyase activity | |
Molecular Function | hyaluronate lyase activity | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | chondroitin sulfate catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChondroitin sulfate ABC exolyase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionQ8A2I1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-14 | |||||
Sequence: MLILSFLCPAFLNA | ||||||
Chain | PRO_0000420124 | 15-1014 | Chondroitin sulfate ABC exolyase | |||
Sequence: QIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGKLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPNAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDRQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPIFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPVREEMKRKFLAMYDHITDQGVAYGSCWGNIHHYGYSVRGLYPAYFLMKDVLREEGKLLEAERTLRWYAITNEVYPKPEGNGIDMDSFNTQTTGRIASILMMEDTPEKLQYLKSFSRWIDYGCRPAPGLAGSFKVDGGAFHHRNNYPAYAVGGLDGATNMIYLFSRTSLAVSELAHRTVKDVLLAMRFYCNKLNFPLSMSGRHPDGQGKLVPMHYAMMAIAGTPDGKGDFDKEMASAYLRLVSSDSSSAEQAPEYMPKVSNAQERKIAKRLVENGFRAESDPQGNLSLGYGCVSVQRRENWSAVARGHSRYLWAAEHYLGHNLYGRYLAHGSLQILTAPPGQTVTPATSGWQQEGFDWNRIPGVTSIHLPLDLLKANVLNVDTFSGMEEMLYSDEAFAGGLSQGKMNGNFGMKLHEHDKYNGTHRARKSYHFIDGMIVCLGSDIENTNTDYPTETTIFQLAVTDKAAHDYWKNNAGEGKVWMDHLGTGYYVPVPARFEKNFPQYSRMQDTGKETKGDWVSLIIDHGKAPKAGSYEYAILPGTDRKTMTAFAKKPAYSVLQQDRNAHILESPSDRITSYVLFETPQSLLPGGLLQRTDTSCLVMVRKESADKVLLTVAQPDLALYRGPSDEAFDKDGKRMERSIYSRPWIDNESGEIPVTVTLKGRWKVAETPFCKVVSEDKKQTVLRFLCKDGASYEVELEK |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,014
- Mass (Da)114,839
- Last updated2003-06-01 v1
- ChecksumA58D5B0085F28355
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE015928 EMBL· GenBank· DDBJ | AAO78430.1 EMBL· GenBank· DDBJ | Genomic DNA |