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Q59288

- CSLA_PEDHD

UniProt

Q59288 - CSLA_PEDHD

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Protein

Chondroitinase-AC

Gene
cslA, chnAC, Phep_0786
Organism
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290)
Status
Reviewed - 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

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
Complete GO annotation...

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
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 – 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.

Miscellaneous databases

EvolutionaryTraceiQ59288.

Family & Domainsi

Sequence similaritiesi

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

« Hide

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

« 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: September 3, 2014
This is version 80 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

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

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