ProGP166 (Chondroitinase-B)

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ProGP ID ProGP166 (Chondroitinase-B)
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, nonpathogenic soil organism.
Gene Information
Gene NamecslB (Phep_0789)
NCBI Gene ID 8251878
GenBank Gene Sequence NC_013061
Protein Information
Protein NameChondroitinase-B
UniProtKB/SwissProt ID Q46079
NCBI RefSeq WP_012780957.1
EMBL-CDSACU03011.1
UniProtKB Sequence >sp|Q46079|CSLB_PEDHD Chondroitinase-B OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GN=cslB PE=1 SV=2 MKMLNKLAGYLLPIMVLLNVAPCLGQVVASNETLYQVVKEVKPGGLVQIADGTYKDVQLI VSNSGKSGLPITIKALNPGKVFFTGDAKVELRGEHLILEGIWFKDGNRAIQAWKSHGPGL VAIYGSYNRITACVFDCFDEANSAYITTSLTEDGKVPQHCRIDHCSFTDKITFDQVINLN NTARAIKDGSVGGPAMYHRVDHCFFSNPQKPGNAGGGIRIGYYRNDIGRCLVDSNLFMRQ DSEAEIITSKSQENVYYGNTYLNCQGTMNFRHGDHQVAINNFYIGNDQRFGYGGMFVWGS RHVIACNYFELSETIKSRGNAALYLNPGAMASEHALAFDMLIANNAFINVNGYAIHFNPL DERRKEYCAANRLKFETPHQLMLKGNLFFKDKPYVYPFFKDDYFIAGKNSWTGNVALGVE KGIPVNISANRSAYKPVKIKDIQPIEGIALDLNALISKGITGKPLSWDEVRPYWLKEMPG TYALTARLSADRAAKFKAVIKRNKEH
Sequence length 506 AA
Subcellular LocationPeriplasm
Function GAG lyase. Cleaves the glycosaminoglycan, dermatan sulfate. EC= 4.2.2.19.
Protein Structure
PDB ID 1DBG, 1DBO, 1OFL, 1OFM
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS234
Experimentally Validated Glycosite(s ) in Mature ProteinS234
Glycosite(s) Annotated Protein Sequence >sp|Q46079|CSLB_PEDHD Chondroitinase-B OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) GN=cslB PE=1 SV=2 MKMLNKLAGYLLPIMVLLNVAPCLGQVVASNETLYQVVKEVKPGGLVQIADGTYKDVQLI VSNSGKSGLPITIKALNPGKVFFTGDAKVELRGEHLILEGIWFKDGNRAIQAWKSHGPGL VAIYGSYNRITACVFDCFDEANSAYITTSLTEDGKVPQHCRIDHCSFTDKITFDQVINLN NTARAIKDGSVGGPAMYHRVDHCFFSNPQKPGNAGGGIRIGYYRNDIGRCLVDS*(234)NLFMRQ DSEAEIITSKSQENVYYGNTYLNCQGTMNFRHGDHQVAINNFYIGNDQRFGYGGMFVWGS RHVIACNYFELSETIKSRGNAALYLNPGAMASEHALAFDMLIANNAFINVNGYAIHFNPL DERRKEYCAANRLKFETPHQLMLKGNLFFKDKPYVYPFFKDDYFIAGKNSWTGNVALGVE KGIPVNISANRSAYKPVKIKDIQPIEGIALDLNALISKGITGKPLSWDEVRPYWLKEMPG TYALTARLSADRAAKFKAVIKRNKEH
Sequence Around Glycosites (21 AA) RNDIGRCLVDSNLFMRQDSEA
Technique(s) used for Glycosylation DetectionDeduced Crystal structure
Technique(s) used for Glycosylated Residue(s) Detection Crystallographic analysis (electron density maps)
Glycan Information
Glycan Annotation Linkages: Man- Ser.
The approx. weight of attached glycan was 1180 Da.
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.
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 Identification1999
Year of Identification Month Wise1999
Year of Validation 1999
ReferenceMichel, G., Pojasek, K., Li, Y., Sulea, T., Linhardt, R.J., Raman, R., Prabhakar, V., Sasisekharan, R. and Cygler, M., 2004. The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery. Journal of Biological Chemistry, 279(31), pp.32882-32896.
Corresponding Author Miroslaw Cygler
ContactBiotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H4P 2R2, Canada.
ReferenceHuang, W., Matte, A., Li, Y., Kim, Y.S., Linhardt, R.J., Su, H. and Cygler, M., 1999. Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 Å resolution. Journal of molecular biology, 294(5), pp.1257-1269.
Corresponding Author Miroslaw Cygler
ContactBiotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montréal, Québec, Canada H4P 2R2.