ProGlyProt ID BC163 Organism Information Organism Name Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) Domain Bacteria Classification Family: Sphingobacteriaceae Order: "Sphingobacteriales" Class: "Sphingobacteria" Division or phylum: "Bacteroidetes" Taxonomic ID (NCBI) 485917 Genome Sequence (s) GeneBank CP001681.1 EMBL CP001681 Gene Information Gene Name cslA (Phep_0786) NCBI Gene ID 8251875 GenBank Gene Sequence 8251875 Protein Information Protein Name Chondroitinase-AC UniProtKB/SwissProt ID Q59288 NCBI RefSeq YP_003091070.1 EMBL-CDS ACU03008.1 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 Location Periplasm 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 Glycosylation Status Glycosylation Type O (Ser) linked Experimentally Validated Glycosite(s) in Full Length Protein S328, S455 Experimentally Validated Glycosite(s ) in Mature Protein S328, 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 Glycosite Sequence Logo seqlogo Glycosite Sequence Logo Technique(s) used for Glycosylation Detection Deduced 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. Technique(s) used for Glycan Identification Crystallographic analysis (electron density maps) Protein Glycosylation linked (PGL) gene(s) OST Gene Name OST NCBI Gene ID OST GenBank Gene Sequence OST Protein Name OST UniProtKB/ SwissProt ID OST NCBI RefSeq OST EMBL-CDS OST UniProtKB Sequence OST EC Number (BRENDA) OST Genome Context Characterized Accessory Gene(s) Information currently not available with us. PGL Additional Links CAZy Literatures Reference(s) 1) Huang, 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, 2359-2372. [PubMed: 11327856] 2) Fethiere, J., Eggimann, B. and Cygler, M. (1999) Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes. J Mol Biol, 288, 635-647. [PubMed: 10329 Additional Comments Sequon features: Identified glycosylation Sequon features: Consensus sequon observed Asp-Ser or Asp-Thr- Thr, at turns. Year of Identification 1996 Year of Validation 1996