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Q59288 (CSLA_PEDHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chondroitinase-AC

EC=4.2.2.5
Alternative name(s):
Chondroitin sulfate AC lyase
Chondroitin-AC eliminase
Chondroitin-AC lyase
Gene names
Name:cslA
Synonyms:chnAC
Ordered Locus Names:Phep_0786
OrganismPedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290) [Complete proteome] [HAMAP]
Taxonomic identifier485917 [NCBI]
Taxonomic lineageBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

chondroitin AC lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59288 [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 

« 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13125 / DSM 2366 / NCIB 9290.
[3]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27583 Genomic DNA. Translation: AAC83383.1.
CP001681 Genomic DNA. Translation: ACU03008.1.
RefSeqYP_003091070.1. NC_013061.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CB8X-ray1.90A23-700[»]
1HM2X-ray2.00A1-700[»]
1HM3X-ray2.10A1-700[»]
1HMUX-ray2.00A1-700[»]
1HMWX-ray2.30A1-700[»]
ProteinModelPortalQ59288.
SMRQ59288. Positions 26-699.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING485917.Phep_0786.

Protein family/group databases

CAZyPL8. Polysaccharide Lyase Family 8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU03008; ACU03008; Phep_0786.
GeneID8251875.
KEGGphe:Phep_0786.
PATRIC22878615. VBIPedHep98714_0803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG04835.
HOGENOMHOG000105747.
OMARGDEYHN.
OrthoDBEOG67DPG9.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15799.
PHEP485917:GHL9-792-MONOMER.

Family and domain databases

Gene3D1.50.10.100. 1 hit.
2.60.220.10. 1 hit.
2.70.98.10. 1 hit.
InterProIPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view]
PfamPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
SUPFAMSSF48230. SSF48230. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ59288.

Entry information

Entry nameCSLA_PEDHD
AccessionPrimary (citable) accession number: Q59288
Secondary accession number(s): C6Y215
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references