ProGP132 (Chondroitinase-AC)

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ProGP ID ProGP132 (Chondroitinase-AC)
Validation Status Characterized
Organism Information
Organism NamePedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290)
Domain Bacteria
Classification Phylum : Bacteroidetes
Class : Sphingobacteriia
Orders : Sphingobaccteriales
Family : Sphingobacteriaceae
Genus : Pedobacter
Species : heparinus
Strain : ATCC 13125 / DSM 2366 / NCIB 9290
Taxonomic ID (NCBI) 485917
Genome Information
GenBank CP001681.1
EMBL CP001681
Organism Additional Information Pedobacter heparinus is a Gram-negative, non-pathogenic soil organism.
Gene Information
Gene NamecslA (Phep_0786)
NCBI Gene ID 8251875
GenBank Gene Sequence NC_013061
Protein Information
Protein NameChondroitinase-AC
UniProtKB/SwissProt ID Q59288
NCBI RefSeq WP_012780954.1
EMBL-CDSACU03008.1
UniProtKB Sequence >sp|Q59288|CSLA_PEDHD Chondroitinase-AC OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GN=cslA PE=1 SV=1 MKKLFVTCIVFFSILSPALLIAQQTGTAELIMKRVMLDLKKPLRNMDKVAEKNLNTLQPD GSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVFDQISKAFKYWYDSD PKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIA LHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFIT GVLKLANYVRDTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKA EKKRLLVAKMIDLKHTEEWADAIARTDSTVAAGYKIEPYHHQFWNGDYVQHLRPAYSFNV RMVSKRTRRSESGNKENLLGRYLSDGATNIQLRGPEYYNIMPVWEWDKIPGITSRDYLTD RPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDSLQAKKAWFFFDKEIVCLGAGINSNA PENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQ SQKGNWFHINNSHSKDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAP KVLANTNQLQAVYHQQLDMVQAIFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAAD PLQKEKTAVLSIRDLKTGKTNRVKIDFPQQEFAGATVELK
Sequence length 700 AA
Subcellular LocationPeriplasm
Function GAG lyase. Eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups.EC= 4.2.2.5.
Protein Structure
PDB ID 1CB8, 1HM2, 1HM3, 1HMU, 1HMW
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS328, S455
Experimentally Validated Glycosite(s ) in Mature ProteinS328, S455
Glycosite(s) Annotated Protein Sequence >sp|Q59288|CSLA_PEDHD Chondroitinase-AC OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GN=cslA PE=1 SV=1 MKKLFVTCIVFFSILSPALLIAQQTGTAELIMKRVMLDLKKPLRNMDKVAEKNLNTLQPD GSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVFDQISKAFKYWYDSD PKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIA LHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFIT GVLKLANYVRDTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKA EKKRLLVAKMIDLKHTEEWADAIARTDS*(328)TVAAGYKIEPYHHQFWNGDYVQHLRPAYSFNV RMVSKRTRRSESGNKENLLGRYLSDGATNIQLRGPEYYNIMPVWEWDKIPGITSRDYLTD RPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDS*(455)LQAKKAWFFFDKEIVCLGAGINSNA PENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQ SQKGNWFHINNSHSKDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAP KVLANTNQLQAVYHQQLDMVQAIFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAAD PLQKEKTAVLSIRDLKTGKTNRVKIDFPQQEFAGATVELK
Sequence Around Glycosites (21 AA) EWADAIARTDSTVAAGYKIEP
GASAYALDYDSLQAKKAWFFF
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Technique(s) used for Glycosylation DetectionDeduced Crystal structure
Technique(s) used for Glycosylated Residue(s) Detection Crystallographic analysis (electron density maps)
Protein Glycosylation- Implication No specifc role has been proposed for O-linked oligosaccharides in chondrotinase AC but their positioning and interaction in the structure of chondroitinase AC in the case of Ser455 attached oligosaccharide, presents a possibility for some role in protein folding, as in mammalian systems.
Glycan Information
Glycan Annotation Linkages: Man-Ser.
The approx. weights of glycans attached to S328 and S455 were 1190Da and 1080 Da, respectively.
Branched heptasaccharide is: galactose-β(1–4)[galactose-α(1–3)](2-O-Me)fucose-β(1–4)xylose-β (1–4)glucuronic acid-α(1–2)[rhamnose-α(1–4)]mannose-α(1-O)Ser.
Only tetrasaccharide glycan observed in crystal structure: Man-(Rha)-GlcUA-Xyl (xylose-β (1–4)glucuronic acid-α(1–2)[rhamnose-α(1–4)]mannose-α(1-O)Ser.
GlyTouCan G07644FE
Technique(s) used for Glycan Identification Crystallographic analysis (electron density maps)
Protein Glycosylation linked (PGL) gene(s)
Additional CommentSequon features: Identified glycosylation Sequon features: Consensus sequon observed Asp-Ser or Asp-Thr- Thr, at turns.
Literature
Year of Identification1996
Year of Identification Month Wise1996.11
Year of Validation 1996
ReferenceHuang, W., Boju, L., Tkalec, L., Su, H., Yang, H.O., Gunay, N.S., Linhardt, R.J., Kim, Y.S., Matte, A. and Cygler, M., 2001. Active site of chondroitin AC lyase revealed by the structure of enzyme− oligosaccharide complexes and mutagenesis. Biochemistry, 40(8), pp.2359-2372.
Corresponding Author Miroslaw Cygler
ContactBiotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Québec H4P 2R2 Canada.
ReferenceFéthière, J., Eggimann, B. and Cygler, M., 1999. Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes. Journal of molecular biology, 288(4), pp.635-647.
Corresponding Author Miroslaw Cygler
ContactBiotechnology Research Institute, 6100 Royalmount Avenue, Montréal, Québec H4P 2R2 Canada.
ReferenceLaliberte, M., Eggimann, B., Zimmermann, J.J.F., Huang, L. and van Halbeek, H., 1996. Determination of the glycosylation sites of glycosaminoglycan lyases from Flavobacterium heparinum. Protein Sci, 5(Suppl 1), p.435s.