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Q59288

- CSLA_PEDHD

UniProt

Q59288 - CSLA_PEDHD

Protein

Chondroitinase-AC

Gene

cslA

Organism
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    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.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei225 – 2251
    Active sitei234 – 2341
    Active sitei288 – 2881
    Metal bindingi405 – 4051Calcium
    Metal bindingi407 – 4071Calcium
    Metal bindingi416 – 4161Calcium
    Metal bindingi417 – 4171Calcium; via carbonyl oxygen

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. chondroitin AC lyase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

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

    Protein family/group databases

    CAZyiPL8. Polysaccharide Lyase Family 8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chondroitinase-AC (EC:4.2.2.5)
    Alternative name(s):
    Chondroitin sulfate AC lyase
    Chondroitin-AC eliminase
    Chondroitin-AC lyase
    Gene namesi
    Name:cslA
    Synonyms:chnAC
    Ordered Locus Names:Phep_0786
    OrganismiPedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290)
    Taxonomic identifieri485917 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter
    ProteomesiUP000000852: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 700678Chondroitinase-ACPRO_0000024927Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi328 – 3281O-linked (Man...)
    Glycosylationi455 – 4551O-linked (Man...)

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi485917.Phep_0786.

    Structurei

    Secondary structure

    1
    700
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 3913
    Helixi46 – 5611
    Beta strandi73 – 753
    Helixi79 – 9315
    Turni98 – 1014
    Helixi103 – 11917
    Helixi126 – 1305
    Helixi132 – 14312
    Helixi144 – 1463
    Beta strandi147 – 1493
    Helixi153 – 1619
    Helixi168 – 1703
    Helixi173 – 18917
    Helixi193 – 20412
    Beta strandi207 – 21711
    Beta strandi225 – 2273
    Turni231 – 2333
    Helixi234 – 24916
    Helixi258 – 27013
    Helixi273 – 2753
    Helixi283 – 2853
    Helixi287 – 2915
    Turni293 – 2964
    Helixi299 – 3013
    Helixi302 – 31110
    Helixi313 – 3153
    Helixi316 – 32611
    Turni332 – 3354
    Beta strandi339 – 3435
    Turni344 – 3474
    Beta strandi348 – 3536
    Beta strandi356 – 3616
    Turni381 – 3844
    Beta strandi385 – 39410
    Helixi395 – 3973
    Helixi401 – 4033
    Helixi406 – 4083
    Beta strandi413 – 4153
    Beta strandi425 – 4273
    Beta strandi436 – 4405
    Beta strandi445 – 4539
    Beta strandi456 – 4649
    Beta strandi469 – 47810
    Beta strandi480 – 49213
    Beta strandi497 – 4993
    Beta strandi502 – 5043
    Beta strandi509 – 5146
    Beta strandi519 – 5224
    Beta strandi525 – 5284
    Beta strandi533 – 5386
    Beta strandi541 – 5466
    Turni547 – 5493
    Beta strandi557 – 57216
    Beta strandi574 – 58411
    Helixi590 – 5934
    Helixi596 – 5983
    Beta strandi601 – 61414
    Turni615 – 6184
    Beta strandi619 – 63214
    Beta strandi635 – 6417
    Beta strandi643 – 6486
    Beta strandi655 – 6595
    Beta strandi666 – 6749
    Turni675 – 6773
    Beta strandi680 – 6867
    Helixi690 – 6923

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CB8X-ray1.90A23-700[»]
    1HM2X-ray2.00A1-700[»]
    1HM3X-ray2.10A1-700[»]
    1HMUX-ray2.00A1-700[»]
    1HMWX-ray2.30A1-700[»]
    ProteinModelPortaliQ59288.
    SMRiQ59288. Positions 26-699.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ59288.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polysaccharide lyase 8 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG04835.
    HOGENOMiHOG000105747.
    OMAiRGDEYHN.
    OrthoDBiEOG67DPG9.

    Family and domain databases

    Gene3Di1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProiIPR008929. 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]
    PfamiPF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48230. SSF48230. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q59288-1 [UniParc]FASTAAdd to Basket

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    MKKLFVTCIV FFSILSPALL IAQQTGTAEL IMKRVMLDLK KPLRNMDKVA    50
    EKNLNTLQPD GSWKDVPYKD DAMTNWLPNN HLLQLETIIQ AYIEKDSHYY 100
    GDDKVFDQIS KAFKYWYDSD PKSRNWWHNE IATPQALGEM LILMRYGKKP 150
    LDEALVHKLT ERMKRGEPEK KTGANKTDIA LHYFYRALLT SDEALLSFAV 200
    KELFYPVQFV HYEEGLQYDY SYLQHGPQLQ ISSYGAVFIT GVLKLANYVR 250
    DTPYALSTEK LAIFSKYYRD SYLKAIRGSY MDFNVEGRGV SRPDILNKKA 300
    EKKRLLVAKM IDLKHTEEWA DAIARTDSTV AAGYKIEPYH HQFWNGDYVQ 350
    HLRPAYSFNV RMVSKRTRRS ESGNKENLLG RYLSDGATNI QLRGPEYYNI 400
    MPVWEWDKIP GITSRDYLTD RPLTKLWGEQ GSNDFAGGVS DGVYGASAYA 450
    LDYDSLQAKK AWFFFDKEIV CLGAGINSNA PENITTTLNQ SWLNGPVIST 500
    AGKTGRGKIT TFKAQGQFWL LHDAIGYYFP EGANLSLSTQ SQKGNWFHIN 550
    NSHSKDEVSG DVFKLWINHG ARPENAQYAY IVLPGINKPE EIKKYNGTAP 600
    KVLANTNQLQ AVYHQQLDMV QAIFYTAGKL SVAGIEIETD KPCAVLIKHI 650
    NGKQVIWAAD PLQKEKTAVL SIRDLKTGKT NRVKIDFPQQ EFAGATVELK 700
    Length:700
    Mass (Da):79,694
    Last modified:November 1, 1996 - v1
    Checksum:iC36B608FCAFFC656
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27583 Genomic DNA. Translation: AAC83383.1.
    CP001681 Genomic DNA. Translation: ACU03008.1.
    RefSeqiWP_012780954.1. NC_013061.1.
    YP_003091070.1. NC_013061.1.

    Genome annotation databases

    EnsemblBacteriaiACU03008; ACU03008; Phep_0786.
    GeneIDi8251875.
    KEGGiphe:Phep_0786.
    PATRICi22878615. VBIPedHep98714_0803.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27583 Genomic DNA. Translation: AAC83383.1 .
    CP001681 Genomic DNA. Translation: ACU03008.1 .
    RefSeqi WP_012780954.1. NC_013061.1.
    YP_003091070.1. NC_013061.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CB8 X-ray 1.90 A 23-700 [» ]
    1HM2 X-ray 2.00 A 1-700 [» ]
    1HM3 X-ray 2.10 A 1-700 [» ]
    1HMU X-ray 2.00 A 1-700 [» ]
    1HMW X-ray 2.30 A 1-700 [» ]
    ProteinModelPortali Q59288.
    SMRi Q59288. Positions 26-699.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 485917.Phep_0786.

    Protein family/group databases

    CAZyi PL8. Polysaccharide Lyase Family 8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACU03008 ; ACU03008 ; Phep_0786 .
    GeneIDi 8251875.
    KEGGi phe:Phep_0786.
    PATRICi 22878615. VBIPedHep98714_0803.

    Phylogenomic databases

    eggNOGi NOG04835.
    HOGENOMi HOG000105747.
    OMAi RGDEYHN.
    OrthoDBi EOG67DPG9.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-15799.
    PHEP485917:GHL9-792-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q59288.

    Family and domain databases

    Gene3Di 1.50.10.100. 1 hit.
    2.60.220.10. 1 hit.
    2.70.98.10. 1 hit.
    InterProi IPR008929. 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 ]
    Pfami PF02278. Lyase_8. 1 hit.
    PF02884. Lyase_8_C. 1 hit.
    PF08124. Lyase_8_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48230. SSF48230. 1 hit.
    SSF49863. SSF49863. 1 hit.
    SSF74650. SSF74650. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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).

    Entry informationi

    Entry nameiCSLA_PEDHD
    AccessioniPrimary (citable) accession number: Q59288
    Secondary accession number(s): C6Y215
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3