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Protein

Chondroitinase-AC

Gene

cslA

Organism
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Ca2+Note: Binds 1 Ca2+ 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15799.
PHEP485917:GHL9-792-MONOMER.
BRENDAi4.2.2.5. 2286.

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 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
KOiK19049.
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

« Hide

        10         20         30         40         50
MKKLFVTCIV FFSILSPALL IAQQTGTAEL IMKRVMLDLK KPLRNMDKVA
60 70 80 90 100
EKNLNTLQPD GSWKDVPYKD DAMTNWLPNN HLLQLETIIQ AYIEKDSHYY
110 120 130 140 150
GDDKVFDQIS KAFKYWYDSD PKSRNWWHNE IATPQALGEM LILMRYGKKP
160 170 180 190 200
LDEALVHKLT ERMKRGEPEK KTGANKTDIA LHYFYRALLT SDEALLSFAV
210 220 230 240 250
KELFYPVQFV HYEEGLQYDY SYLQHGPQLQ ISSYGAVFIT GVLKLANYVR
260 270 280 290 300
DTPYALSTEK LAIFSKYYRD SYLKAIRGSY MDFNVEGRGV SRPDILNKKA
310 320 330 340 350
EKKRLLVAKM IDLKHTEEWA DAIARTDSTV AAGYKIEPYH HQFWNGDYVQ
360 370 380 390 400
HLRPAYSFNV RMVSKRTRRS ESGNKENLLG RYLSDGATNI QLRGPEYYNI
410 420 430 440 450
MPVWEWDKIP GITSRDYLTD RPLTKLWGEQ GSNDFAGGVS DGVYGASAYA
460 470 480 490 500
LDYDSLQAKK AWFFFDKEIV CLGAGINSNA PENITTTLNQ SWLNGPVIST
510 520 530 540 550
AGKTGRGKIT TFKAQGQFWL LHDAIGYYFP EGANLSLSTQ SQKGNWFHIN
560 570 580 590 600
NSHSKDEVSG DVFKLWINHG ARPENAQYAY IVLPGINKPE EIKKYNGTAP
610 620 630 640 650
KVLANTNQLQ AVYHQQLDMV QAIFYTAGKL SVAGIEIETD KPCAVLIKHI
660 670 680 690 700
NGKQVIWAAD PLQKEKTAVL SIRDLKTGKT NRVKIDFPQQ EFAGATVELK
Length:700
Mass (Da):79,694
Last modified:November 1, 1996 - v1
Checksum:iC36B608FCAFFC656
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27583 Genomic DNA. Translation: AAC83383.1.
CP001681 Genomic DNA. Translation: ACU03008.1.
RefSeqiWP_012780954.1. NZ_AQGK01000003.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27583 Genomic DNA. Translation: AAC83383.1.
CP001681 Genomic DNA. Translation: ACU03008.1.
RefSeqiWP_012780954.1. NZ_AQGK01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

STRINGi485917.Phep_0786.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiNOG04835.
HOGENOMiHOG000105747.
KOiK19049.
OMAiRGDEYHN.
OrthoDBiEOG67DPG9.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15799.
PHEP485917:GHL9-792-MONOMER.
BRENDAi4.2.2.5. 2286.

Miscellaneous databases

EvolutionaryTraceiQ59288.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.