| 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 |
