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Reviewed, UniProtKB/Swiss-Prot Q59288 (CSLA_PEDHE)

Last modified November 25, 2008. Version 49. 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-AC
    EC=4.2.2.5
Alternative name(s):
    Chondroitin-AC lyase
    Chondroitin sulfate AC lyase
    Chondroitin-AC eliminase
Gene names
Name: cslA
Synonyms: chnAC
OrganismPedobacter heparinus (Flavobacterium heparinum)
Taxonomic identifier984 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

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Protein attributes

Sequence length700 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)

Catalytic activity

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.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

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Ontologies

Keywords

   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

chondroitin AC 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 – 2222
Chain23 – 700678Chondroitinase-AC
PRO_0000024927

Sites

Active site2251
Active site2341
Active site2881
Metal binding4051Calcium
Metal binding4071Calcium
Metal binding4161Calcium
Metal binding4171Calcium; via carbonyl oxygen

Amino acid modifications

Glycosylation3281O-linked (Man...)
Glycosylation4551O-linked (Man...)

Secondary structure

1 ...................................................................................................................... 700
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q59288-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C36B608FCAFFC656

FASTA70079,694
        10         20         30         40         50         60 
MKKLFVTCIV FFSILSPALL IAQQTGTAEL IMKRVMLDLK KPLRNMDKVA EKNLNTLQPD 

        70         80         90        100        110        120 
GSWKDVPYKD DAMTNWLPNN HLLQLETIIQ AYIEKDSHYY GDDKVFDQIS KAFKYWYDSD 

       130        140        150        160        170        180 
PKSRNWWHNE IATPQALGEM LILMRYGKKP LDEALVHKLT ERMKRGEPEK KTGANKTDIA 

       190        200        210        220        230        240 
LHYFYRALLT SDEALLSFAV KELFYPVQFV HYEEGLQYDY SYLQHGPQLQ ISSYGAVFIT 

       250        260        270        280        290        300 
GVLKLANYVR DTPYALSTEK LAIFSKYYRD SYLKAIRGSY MDFNVEGRGV SRPDILNKKA 

       310        320        330        340        350        360 
EKKRLLVAKM IDLKHTEEWA DAIARTDSTV AAGYKIEPYH HQFWNGDYVQ HLRPAYSFNV 

       370        380        390        400        410        420 
RMVSKRTRRS ESGNKENLLG RYLSDGATNI QLRGPEYYNI MPVWEWDKIP GITSRDYLTD 

       430        440        450        460        470        480 
RPLTKLWGEQ GSNDFAGGVS DGVYGASAYA LDYDSLQAKK AWFFFDKEIV CLGAGINSNA 

       490        500        510        520        530        540 
PENITTTLNQ SWLNGPVIST AGKTGRGKIT TFKAQGQFWL LHDAIGYYFP EGANLSLSTQ 

       550        560        570        580        590        600 
SQKGNWFHIN NSHSKDEVSG DVFKLWINHG ARPENAQYAY IVLPGINKPE EIKKYNGTAP 

       610        620        630        640        650        660 
KVLANTNQLQ AVYHQQLDMV QAIFYTAGKL SVAGIEIETD KPCAVLIKHI NGKQVIWAAD 

       670        680        690        700 
PLQKEKTAVL SIRDLKTGKT NRVKIDFPQQ EFAGATVELK

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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]"Crystal structure of chondroitin AC lyase, a representative of a family of glycosaminoglycan degrading enzymes."
Fethiere J., Eggimann B., Cygler M.
J. Mol. Biol. 288:635-647(1999) [PubMed: 10329169] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[3]"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).

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Cross-references

Sequence databases

U27583 Genomic DNA. Translation: AAC83383.1.

3D structure databases

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EntryMethodResolution (Å)