A0A0G4Q5T7 · A0A0G4Q5T7_9GAMM

  • Protein
    Chondroitin sulfate ABC lyase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Broad-specificity glycosaminoglycan lyase.

Features

Showing features for binding site, active site.

110241002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site211Ca2+ (UniProtKB | ChEBI)
Active site389Proton acceptor
Active site501Proton acceptor
Active site508Proton donor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functioncarbohydrate binding
Molecular Functionchondroitin-sulfate-ABC endolyase activity
Molecular Functionmetal ion binding
Biological Processcarbohydrate metabolic process
Biological Processglycosaminoglycan catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chondroitin sulfate ABC lyase
  • Alternative names
    • Chondroitin ABC eliminase
    • Chondroitin ABC lyase
    • Chondroitinase ABC

Gene names

    • ORF names
      BN1804_01321

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CSUR P1867
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Morganellaceae > Proteus

Accessions

  • Primary accession
    A0A0G4Q5T7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_500519610525-1024Chondroitin sulfate ABC lyase

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain40-230Lyase N-terminal
Domain248-603Lyase catalytic
Domain629-878Polysaccharide lyase family 8 central
Region839-859Disordered
Domain901-960Polysaccharide lyase family 8 C-terminal

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,024
  • Mass (Da)
    115,112
  • Last updated
    2015-09-16 v1
  • Checksum
    E9B8F4B608480277
MPIFRFTALAITLGLLSAPYNAMAATSNPAFDPKNLMQSEIYHFAQSNPLADFSSDKNSTLTLSDKRSIMGNQSLLWKWKGGSSFTLHKKIIVPTDKEASKAWGRASTPVLSFWLYNEKPIDGYLTIDFGEKLKSTSEAQAGFKVKLNFTGWRAVGISLNNDLENREMLLNTMNTSSDGTQDSIGRSLGANVDSIRFKAPSNVGQGEIYIDRIMFSIDDARYQWSDYQVKTRLSEPEIQFNNVQPQLPVTPENLAAIDLIRQRLINEFVGGEKETNLALEENISKLKSDFDALNIHALADGGTQGRHLITDKQTIIYQPEHLNSQDKPLFDNYVILGNYTTLMFNISRAYVLEKDPTQKAQLKQMYLLMTKHLLDQGFVKGSALVTTHHWGYSSRWWYISTLLMSDALKEANLQTQVYDSLLWYSREFKSSFDMKVGANSSDLDYFNTLSRQHLALLLLEPDDQKRINLVNTFSHYITGALTQVPPGSKDGLRPDGTAWRHEGNYPGYSFPAFKNASQLIYLLRATPFAVGESGWNNLKKAMVSAWIYSNPEVGLPLAGRHPFNSPSLKSIAQGYYWLAMSAKPSPDKKLASIYLAISDKTQNESSAIFGETIAPAALPQGFYAFNGGAFGIHRWQDKMVTLKAYNTNVWSSEIYNKDNRYGRYQSHGVAQIVSNGSQLSQGYQQEGWDWNRMPGATTIHLPLKELDSPKPHTLMQRGERGFSGTSALDGKYGMMAFDLIYPANLERFDPNFTAQKSVLAADNHLIFIGSNINSSDKNKNVETTLFQHAITPTLNTIWINGQKIEAIPYQTTLKQGDWLIDSNGNGYLITQAEKVNVSRQHQTSAENKNRQPTEGDFSSTWIDHSVQPKDSSYEYMVFLDATPEKMGEMAQKFRENNGLYQVLRKDKDVHIIYDKLSNVTGYAFYQSASVEDKWIKKVDKPAIVMTHHQGNSLTVSAVTPDLNMTRQKAATAVTINVIVKGKWQPTEPTDKNNKVKYHVSGDNTELTFTSYFGIPQEIKLSPLS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CVRY01000002
EMBL· GenBank· DDBJ
CRL61130.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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