Q8A2I1 · CABC2_BACTN

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

  • Exolytic removal of Delta4-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.
    EC:4.2.2.21 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

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.

TypeIDPosition(s)Description
Binding site24Ca2+ (UniProtKB | ChEBI)
Binding site26Ca2+ (UniProtKB | ChEBI)
Binding site50Ca2+ (UniProtKB | ChEBI)
Binding site53Ca2+ (UniProtKB | ChEBI)
Binding site161Ca2+ (UniProtKB | ChEBI)
Site172Important for catalytic activity against all substrates
Site344Important for catalytic activity against dermatan sulfate substrate
Active site345Proton acceptor
Active site454Proton acceptor
Active site461Proton donor
Site514Transition state stabilizer
Site628Important for catalytic activity against all substrates

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentperiplasmic space
Molecular Functioncarbohydrate binding
Molecular Functioncarbon-oxygen lyase activity, acting on polysaccharides
Molecular Functionchondroitin AC lyase activity
Molecular Functionchondroitin B lyase activity
Molecular Functionchondroitin-sulfate-ABC endolyase activity
Molecular Functionchondroitin-sulfate-ABC exolyase activity
Molecular Functionhyaluronate lyase activity
Molecular Functionmetal ion binding
Biological Processcarbohydrate metabolic process
Biological Processchondroitin sulfate catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • PL8Polysaccharide Lyase Family 8

Names & Taxonomy

Protein names

  • Recommended name
    Chondroitin sulfate ABC exolyase
  • EC number
  • Alternative names
    • Chondroitin ABC exoeliminase
    • Chondroitin ABC lyase II
    • Chondroitin sulfate ABC lyase II
      (ChS ABC lyase II
      )
    • Chondroitinase ABC II
      (cABC II
      )
    • Exochondroitinase ABC

Gene names

    • Name
      chonabc
    • Ordered locus names
      BT_3324

Organism names

Accessions

  • Primary accession
    Q8A2I1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-14
ChainPRO_000042012415-1014Chondroitin sulfate ABC exolyase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,014
  • Mass (Da)
    114,839
  • Last updated
    2003-06-01 v1
  • Checksum
    A58D5B0085F28355
MLILSFLCPAFLNAQIVTDERMFSFEEPQLPACITGVQSQLGISGAHYKDGKHSLEWTFEPNGKLELRKDLKFEKKDPTGKDLYLSAFIVWIYNEQPQDAAIEFEFLKDGRKCASFPFGINFKGWRAAWVCYERDMQGTPEEGMNELRIVAPNAKGRLFIDHLITATKVDARQQTADLQVPFVNAGTTNHWLVLYKHSLLKPDIELTPVSDRQRQEMKLLEKRFRDMIYTKGKVTEKEAETIRKKYDLYQITYKDGQVSGVPIFMVRASEAYERMIPDWDKDMLTKMGIEMRAYFDLMKRIAVAYNNSEAGSPVREEMKRKFLAMYDHITDQGVAYGSCWGNIHHYGYSVRGLYPAYFLMKDVLREEGKLLEAERTLRWYAITNEVYPKPEGNGIDMDSFNTQTTGRIASILMMEDTPEKLQYLKSFSRWIDYGCRPAPGLAGSFKVDGGAFHHRNNYPAYAVGGLDGATNMIYLFSRTSLAVSELAHRTVKDVLLAMRFYCNKLNFPLSMSGRHPDGQGKLVPMHYAMMAIAGTPDGKGDFDKEMASAYLRLVSSDSSSAEQAPEYMPKVSNAQERKIAKRLVENGFRAESDPQGNLSLGYGCVSVQRRENWSAVARGHSRYLWAAEHYLGHNLYGRYLAHGSLQILTAPPGQTVTPATSGWQQEGFDWNRIPGVTSIHLPLDLLKANVLNVDTFSGMEEMLYSDEAFAGGLSQGKMNGNFGMKLHEHDKYNGTHRARKSYHFIDGMIVCLGSDIENTNTDYPTETTIFQLAVTDKAAHDYWKNNAGEGKVWMDHLGTGYYVPVPARFEKNFPQYSRMQDTGKETKGDWVSLIIDHGKAPKAGSYEYAILPGTDRKTMTAFAKKPAYSVLQQDRNAHILESPSDRITSYVLFETPQSLLPGGLLQRTDTSCLVMVRKESADKVLLTVAQPDLALYRGPSDEAFDKDGKRMERSIYSRPWIDNESGEIPVTVTLKGRWKVAETPFCKVVSEDKKQTVLRFLCKDGASYEVELEK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE015928
EMBL· GenBank· DDBJ
AAO78430.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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