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Protein

Chondroitinase-AC

Gene

cslA

Organism
Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
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)DescriptionActionsGraphical viewLength
Active sitei2251
Active sitei2341
Active sitei2881
Metal bindingi405Calcium1
Metal bindingi407Calcium1
Metal bindingi416Calcium1
Metal bindingi417Calcium; via carbonyl oxygen1

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.
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 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Taxonomic identifieri485917 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter
Proteomesi
  • UP000000852 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000002492723 – 700Chondroitinase-ACAdd BLAST678

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi328O-linked (Man...)1
Glycosylationi455O-linked (Man...)1

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi485917.Phep_0786.

Structurei

Secondary structure

1700
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 39Combined sources13
Helixi46 – 56Combined sources11
Beta strandi73 – 75Combined sources3
Helixi79 – 93Combined sources15
Turni98 – 101Combined sources4
Helixi103 – 119Combined sources17
Helixi126 – 130Combined sources5
Helixi132 – 143Combined sources12
Helixi144 – 146Combined sources3
Beta strandi147 – 149Combined sources3
Helixi153 – 161Combined sources9
Helixi168 – 170Combined sources3
Helixi173 – 189Combined sources17
Helixi193 – 204Combined sources12
Beta strandi207 – 217Combined sources11
Beta strandi225 – 227Combined sources3
Turni231 – 233Combined sources3
Helixi234 – 249Combined sources16
Helixi258 – 270Combined sources13
Helixi273 – 275Combined sources3
Helixi283 – 285Combined sources3
Helixi287 – 291Combined sources5
Turni293 – 296Combined sources4
Helixi299 – 301Combined sources3
Helixi302 – 311Combined sources10
Helixi313 – 315Combined sources3
Helixi316 – 326Combined sources11
Turni332 – 335Combined sources4
Beta strandi339 – 343Combined sources5
Turni344 – 347Combined sources4
Beta strandi348 – 353Combined sources6
Beta strandi356 – 361Combined sources6
Turni381 – 384Combined sources4
Beta strandi385 – 394Combined sources10
Helixi395 – 397Combined sources3
Helixi401 – 403Combined sources3
Helixi406 – 408Combined sources3
Beta strandi413 – 415Combined sources3
Beta strandi425 – 427Combined sources3
Beta strandi436 – 440Combined sources5
Beta strandi445 – 453Combined sources9
Beta strandi456 – 464Combined sources9
Beta strandi469 – 478Combined sources10
Beta strandi480 – 492Combined sources13
Beta strandi497 – 499Combined sources3
Beta strandi502 – 504Combined sources3
Beta strandi509 – 514Combined sources6
Beta strandi519 – 522Combined sources4
Beta strandi525 – 528Combined sources4
Beta strandi533 – 538Combined sources6
Beta strandi541 – 546Combined sources6
Turni547 – 549Combined sources3
Beta strandi557 – 572Combined sources16
Beta strandi574 – 584Combined sources11
Helixi590 – 593Combined sources4
Helixi596 – 598Combined sources3
Beta strandi601 – 614Combined sources14
Turni615 – 618Combined sources4
Beta strandi619 – 632Combined sources14
Beta strandi635 – 641Combined sources7
Beta strandi643 – 648Combined sources6
Beta strandi655 – 659Combined sources5
Beta strandi666 – 674Combined sources9
Turni675 – 677Combined sources3
Beta strandi680 – 686Combined sources7
Helixi690 – 692Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59288.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000105747.
KOiK19049.
OMAiRGDEYHN.
OrthoDBiPOG091H03FL.

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. GH-type_carb-bd.
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
PDB 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.
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

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000105747.
KOiK19049.
OMAiRGDEYHN.
OrthoDBiPOG091H03FL.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15799.
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. GH-type_carb-bd.
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...

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: November 2, 2016
This is version 95 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

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 one 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.