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Q46079 (CSLB_PEDHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chondroitinase-B
EC=4.2.2.19
Alternative name(s):
Chondroitin sulfate B lyase
Chondroitin-B eliminase
Chondroitin-B lyase
Gene names
Name:cslB
Ordered Locus Names:Phep_0789
OrganismPedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) [Complete proteome] [HAMAP]
Taxonomic identifier485917 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Sphingobacteriia › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

Protein attributes

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

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.

Ontologies

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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.3
Mutagenesis2721H → A: Partial loss of activity. Ref.3
Mutagenesis3331E → A: Partial loss of activity. Ref.3
Mutagenesis3631R → A: No effect. Ref.3
Mutagenesis3641R → A: Partial loss of activity and altered product profile. Ref.3
Sequence conflict1951A → G in AAC83384. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46079 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: 454B93EC0AACD2A3

FASTA50656,337
        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 VGGPAMYHRV 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

References

« Hide 'large scale' 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].
[2]"Complete genome sequence of Pedobacter heparinus type strain (HIM 762-3)."
Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A. expand/collapse author list , Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.
Stand. Genomic Sci. 1:54-62(2009) [PubMed: 21304637] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13125 / DSM 2366 / NCIB 9290.
[3]"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.
[4]"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).
[5]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U27584 Genomic DNA. Translation: AAC83384.1.
CP001681 Genomic DNA. Translation: ACU03011.1.
RefSeqYP_003091073.1. NC_013061.1.

3D structure databases

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

Protein-protein interaction databases

STRINGQ46079.

Protein family/group databases

CAZyPL6. Polysaccharide Lyase Family 6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8251878.
GenomeReviewsGene locus Phep_0789 in contig CP001681_GR.
KEGGphe:Phep_0789.
PATRIC22878621. VBIPedHep98714_0806.

Organism-specific databases

CMRSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15800.

Family and domain databases

InterProIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCSLB_PEDHD
AccessionPrimary (citable) accession number: Q46079
Secondary accession number(s): C6Y218
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 3, 2009
Last modified: January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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