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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)
 
 
Genome Sequence(s)
GenBank
EMBL
Organism Additional Information
Pedobacter heparinus is a Gram-negative, nonpathogenic soil organism.
 
 
Gene Information
Gene Name
cslA (Phep_0786)
NCBI Gene ID
GenBank Gene Sequence
 
 
Protein Information
Protein Name
Chondroitinase-AC
UniProtKB/SwissProt ID
NCBI RefSeq
EMBL-CDS
UniProtKB Sequence
>sp|Q59288|CSLA_PEDHD Chondroitinase-AC OS=Pedobacter heparinus (strain ATCC 131
25 / DSM 2366 / NCIB 9290) GN=cslA PE=1 SV=1 MKKLFVTCIVFFSILSPALLIAQQTGTAELI
MKRVMLDLKKPLRNMDKVAEKNLNTLQPD GSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDKVF
DQISKAFKYWYDSD PKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTDIA
LHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFIT GVLKLANYVRDTPYA
LSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKA EKKRLLVAKMIDLKHTEEWADAIARTDSTV
AAGYKIEPYHHQFWNGDYVQHLRPAYSFNV RMVSKRTRRSESGNKENLLGRYLSDGATNIQLRGPEYYNIMPVWE
WDKIPGITSRDYLTD RPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDSLQAKKAWFFFDKEIVCLGAGINSNA
PENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFPEGANLSLSTQ SQKGNWFHINNSHS
KDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAP KVLANTNQLQAVYHQQLDMVQAIFYTAGK
LSVAGIEIETDKPCAVLIKHINGKQVIWAAD 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
 
 
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 131
25 / DSM 2366 / NCIB 9290) GN=cslA PE=1 SV=1 MKKLFVTCIVFFSILSPALLIAQQTGTAEL
IMKRVMLDLKKPLRNMDKVAEKNLNTLQPD GSWKDVPYKDDAMTNWLPNNHLLQLETIIQAYIEKDSHYYGDDK
VFDQISKAFKYWYDSD PKSRNWWHNEIATPQALGEMLILMRYGKKPLDEALVHKLTERMKRGEPEKKTGANKTD
IA LHYFYRALLTSDEALLSFAVKELFYPVQFVHYEEGLQYDYSYLQHGPQLQISSYGAVFIT GVLKLANYVR
DTPYALSTEKLAIFSKYYRDSYLKAIRGSYMDFNVEGRGVSRPDILNKKA EKKRLLVAKMIDLKHTEEWADAIA
RTDS*(328)TVAAGYKIEPYHHQFWNGDYVQHLRPAYSFNV RMVSKRTRRSESGNKENLLGRYLSDGATNI
QLRGPEYYNIMPVWEWDKIPGITSRDYLTD RPLTKLWGEQGSNDFAGGVSDGVYGASAYALDYDS*(455)L
QAKKAWFFFDKEIVCLGAGINSNA PENITTTLNQSWLNGPVISTAGKTGRGKITTFKAQGQFWLLHDAIGYYFP
EGANLSLSTQ SQKGNWFHINNSHSKDEVSGDVFKLWINHGARPENAQYAYIVLPGINKPEEIKKYNGTAP KV
LANTNQLQAVYHQQLDMVQAIFYTAGKLSVAGIEIETDKPCAVLIKHINGKQVIWAAD PLQKEKTAVLSIRDLK
TGKTNRVKIDFPQQEFAGATVELK
Sequence Around Glycosites (21 AA)
EWADAIARTDSTVAAGYKIEP
GASAYALDYDSLQAKKAWFFF
Glycosite Sequence Logo
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)
Characterized Accessory Gene(s)
Information currently not available with us.
PGL Additional Links
 
 
Literature
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: 10329169]
3) M. Laliberté, B. Eggimann, J. Zimmerman, L. Huang and H. van Halbeek. (1996) Determination of the glycosylation sites of glycosaminoglycan lyases from Flavobacterium heparinum. Protein Sci.1996, 5 (suppl. 1) 435-s.
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
 
 
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