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Reviewed, UniProtKB/Swiss-Prot Q46079 (CSLB_PEDHE)

Last modified May 26, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chondroitinase-B
    EC=4.2.2.19
Alternative name(s):
    Chondroitin-B lyase
    Chondroitin sulfate B lyase
    Chondroitin-B eliminase
Gene names
Name: cslB
OrganismPedobacter heparinus (Flavobacterium heparinum)
Taxonomic identifier984 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

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Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Cleaves the glycosaminoglycan, dermatan sulfate.

Catalytic activity

Eliminative cleavage of dermatan sulfate containing (1->4)-beta-D-hexosaminyl and (1->3)-beta-D-glucurosonyl or (1->3)-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (Delta-UA-GalNAc-4S).

Subunit structure

Monomer.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

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Ontologies

Keywords
   DomainSignal
   Molecular functionLyase
   PTMGlycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Gene Ontology (GO)
   Molecular functionchondroitin B lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 506481Chondroitinase-B
PRO_0000024928

Sites

Active site2501
Active site2721
Active site3331

Amino acid modifications

Modified residue261Pyrrolidone carboxylic acid
Glycosylation2341O-linked (Man...)

Experimental info

Mutagenesis2501K → A: Complete loss of activity. Ref.2
Mutagenesis2721H → A: Partial loss of activity. Ref.2
Mutagenesis3331E → A: Partial loss of activity. Ref.2
Mutagenesis3631R → A: No effect. Ref.2
Mutagenesis3641R → A: Partial loss of activity and altered product profile. Ref.2

Secondary structure

1 ........................................................................................................ 506
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q46079-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 84D59270370CD101

FASTA50656,322
        10         20         30         40         50         60 
MKMLNKLAGY LLPIMVLLNV APCLGQVVAS NETLYQVVKE VKPGGLVQIA DGTYKDVQLI 

        70         80         90        100        110        120 
VSNSGKSGLP ITIKALNPGK VFFTGDAKVE LRGEHLILEG IWFKDGNRAI QAWKSHGPGL 

       130        140        150        160        170        180 
VAIYGSYNRI TACVFDCFDE ANSAYITTSL TEDGKVPQHC RIDHCSFTDK ITFDQVINLN 

       190        200        210        220        230        240 
NTARAIKDGS VGGPGMYHRV DHCFFSNPQK PGNAGGGIRI GYYRNDIGRC LVDSNLFMRQ 

       250        260        270        280        290        300 
DSEAEIITSK SQENVYYGNT YLNCQGTMNF RHGDHQVAIN NFYIGNDQRF GYGGMFVWGS 

       310        320        330        340        350        360 
RHVIACNYFE LSETIKSRGN AALYLNPGAM ASEHALAFDM LIANNAFINV NGYAIHFNPL 

       370        380        390        400        410        420 
DERRKEYCAA NRLKFETPHQ LMLKGNLFFK DKPYVYPFFK DDYFIAGKNS WTGNVALGVE 

       430        440        450        460        470        480 
KGIPVNISAN RSAYKPVKIK DIQPIEGIAL DLNALISKGI TGKPLSWDEV RPYWLKEMPG 

       490        500 
TYALTARLSA DRAAKFKAVI KRNKEH

« Hide

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References

[1]"Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum."
Tkalec A.L., Fink D., Blain F., Zhang-Sun G., Laliberte M., Bennett D.C., Gu K., Zimmermann J.J.F., Su H.
Appl. Environ. Microbiol. 66:29-35(2000) [PubMed: 10618199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13125 / DSM 2366 / IFO 12017 / LMG 10339 / NCIB 9290.
[2]"Biochemical characterization of the chondroitinase B active site."
Pojasek K., Raman R., Kiley P., Venkataraman G., Sasisekharan R.
J. Biol. Chem. 277:31179-31186(2002) [PubMed: 12063249] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-250; HIS-272; GLU-333; ARG-363 AND ARG-364.
[3]"Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 A resolution."
Huang W., Matte A., Li Y., Kim Y.S., Linhardt R.J., Su H., Cygler M.
J. Mol. Biol. 294:1257-1269(1999) [PubMed: 10600383] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[4]"Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis."
Huang W., Boju L., Tkalec A.L., Su H., Yang H.O., Gunay N.S., Linhardt R.J., Kim Y.S., Matte A., Cygler M.
Biochemistry 40:2359-2372(2001) [PubMed: 11327856] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

U27584 Genomic DNA. Translation: AAC83384.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DBGX-ray1.70A1-506[»]
1DBOX-ray1.70A1-506[»]
1OFLX-ray1.70A27-506[»]
1OFMX-ray1.80A27-506[»]
ModBaseSearch...

Protein family/group databases

CAZyPL6. Polysaccharide Lyase Family 6.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameCSLB_PEDHE
AccessionPrimary (citable) accession number: Q46079
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 1, 1996
Last modified: May 26, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents