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Protein

Chondroitin sulfate ABC endolyase

Gene
N/A
Organism
Proteus vulgaris
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).3 Publications

Catalytic activityi

Endolytic cleavage of (1->4)-beta-galactosaminic bonds between N-acetylgalactosamine and either D-glucuronic acid or L-iduronic acid to produce a mixture of Delta(4)-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta(4)-unsaturated tetra- and disaccharides.4 Publications

Enzyme regulationi

Is inhibited by Zn2+, Ni2+, Fe2+ and Cu2+.1 Publication

Kineticsi

  1. KM=66 µM for chondroitin 6-sulfate2 Publications
  2. KM=1.2 µM for chondroitin 6-sulfate2 Publications
  3. KM=1.5 µM for chondroitin 4-sulfate2 Publications
  4. KM=2.5 µM for dermatan sulfate2 Publications
  1. Vmax=310 µmol/min/mg enzyme with chondroitin 6-sulfate as substrate2 Publications

pH dependencei

Optimum pH is 8. Is essentially inactive at pH 9.0.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi43Sodium or calcium; via carbonyl oxygen1
Metal bindingi70Sodium or calcium; via carbonyl oxygen1
Metal bindingi73Sodium or calcium; via carbonyl oxygen1
Metal bindingi211Sodium or calcium1
Active sitei501Proton acceptor2 Publications1
Active sitei508Proton donorSequence analysis1
Sitei560Transition state stabilizerSequence analysis1
Sitei653Important for catalytic activity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding, Sodium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15788.
BRENDAi4.2.2.20. 5049.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin sulfate ABC endolyase (EC:4.2.2.20)
Alternative name(s):
Chondroitin ABC endoeliminase
Chondroitin ABC lyase I
Chondroitin sulfate ABC lyase I
Short name:
ChS ABC lyase I
Chondroitinase ABC I
Short name:
cABC I
Endochondroitinase ABC
INN: Condoliase
OrganismiProteus vulgaris
Taxonomic identifieri585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi500R → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with highly reduced catalytic efficiency. 2 Publications1
Mutagenesisi501H → A, K or R: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi508Y → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi508Y → F: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with greatly reduced catalytic efficiency. 2 Publications1
Mutagenesisi560R → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi561H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication1
Mutagenesisi653E → A or D: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications1
Mutagenesisi653E → Q: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 2 Publications1
Mutagenesisi712H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000002492925 – 1021Chondroitin sulfate ABC endolyaseAdd BLAST997

Proteomic databases

PRIDEiP59807.

Expressioni

Inductioni

By chondroitin sulfate or its degraded products.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP59807. 2 interactors.

Structurei

Secondary structure

11021
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 42Combined sources3
Beta strandi46 – 48Combined sources3
Turni49 – 52Combined sources4
Beta strandi59 – 67Combined sources9
Beta strandi69 – 72Combined sources4
Beta strandi74 – 80Combined sources7
Beta strandi84 – 88Combined sources5
Helixi96 – 103Combined sources8
Beta strandi105 – 119Combined sources15
Beta strandi122 – 132Combined sources11
Beta strandi140 – 146Combined sources7
Beta strandi151 – 158Combined sources8
Turni159 – 161Combined sources3
Beta strandi194 – 198Combined sources5
Beta strandi204 – 219Combined sources16
Helixi251 – 269Combined sources19
Helixi283 – 291Combined sources9
Helixi313 – 317Combined sources5
Helixi319 – 321Combined sources3
Helixi324 – 330Combined sources7
Beta strandi333 – 335Combined sources3
Helixi336 – 352Combined sources17
Helixi356 – 375Combined sources20
Helixi390 – 403Combined sources14
Helixi405 – 410Combined sources6
Helixi414 – 424Combined sources11
Helixi425 – 428Combined sources4
Helixi429 – 432Combined sources4
Turni438 – 441Combined sources4
Helixi443 – 448Combined sources6
Helixi450 – 458Combined sources9
Helixi463 – 482Combined sources20
Beta strandi490 – 492Combined sources3
Beta strandi498 – 500Combined sources3
Helixi506 – 523Combined sources18
Helixi532 – 547Combined sources16
Beta strandi549 – 553Combined sources5
Helixi555 – 557Combined sources3
Helixi568 – 571Combined sources4
Helixi572 – 579Combined sources8
Helixi588 – 598Combined sources11
Helixi602 – 609Combined sources8
Beta strandi621 – 625Combined sources5
Helixi626 – 628Combined sources3
Beta strandi630 – 635Combined sources6
Beta strandi638 – 643Combined sources6
Beta strandi649 – 651Combined sources3
Helixi662 – 664Combined sources3
Beta strandi667 – 676Combined sources10
Helixi679 – 681Combined sources3
Beta strandi697 – 699Combined sources3
Helixi703 – 706Combined sources4
Beta strandi709 – 712Combined sources4
Beta strandi719 – 721Combined sources3
Beta strandi724 – 728Combined sources5
Turni729 – 731Combined sources3
Beta strandi732 – 740Combined sources9
Beta strandi753 – 761Combined sources9
Beta strandi764 – 773Combined sources10
Turni775 – 780Combined sources6
Beta strandi781 – 789Combined sources9
Beta strandi792 – 794Combined sources3
Beta strandi797 – 799Combined sources3
Beta strandi802 – 804Combined sources3
Beta strandi807 – 813Combined sources7
Beta strandi818 – 820Combined sources3
Beta strandi826 – 831Combined sources6
Beta strandi835 – 845Combined sources11
Turni847 – 849Combined sources3
Beta strandi852 – 863Combined sources12
Helixi864 – 866Combined sources3
Beta strandi867 – 878Combined sources12
Helixi883 – 894Combined sources12
Beta strandi898 – 914Combined sources17
Turni915 – 918Combined sources4
Beta strandi919 – 926Combined sources8
Beta strandi933 – 948Combined sources16
Beta strandi953 – 958Combined sources6
Beta strandi966 – 968Combined sources3
Beta strandi973 – 981Combined sources9
Beta strandi983 – 986Combined sources4
Beta strandi993 – 997Combined sources5
Beta strandi1000 – 1008Combined sources9
Beta strandi1013 – 1019Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HN0X-ray1.90A1-1021[»]
SMRiP59807.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59807.

Family & Domainsi

Domaini

Consists of three domains. The middle domain contains the catalytic site in a wide-open cleft.1 Publication

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
2.60.120.410. 1 hit.
2.60.220.10. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR008929. Chondroitin_lyas.
IPR024200. Chondroitinase_ABC_I.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR011071. Lyase_8-like_C.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
IPR015177. Lyase_catalyt.
IPR015176. Lyase_N.
[Graphical view]
PfamiPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF09093. Lyase_catalyt. 1 hit.
PF09092. Lyase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF034515. Chondroitinase. 1 hit.
SUPFAMiSSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 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.

P59807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIFRFTALA MTLGLLSAPY NAMAATSNPA FDPKNLMQSE IYHFAQNNPL
60 70 80 90 100
ADFSSDKNSI LTLSDKRSIM GNQSLLWKWK GGSSFTLHKK LIVPTDKEAS
110 120 130 140 150
KAWGRSSTPV FSFWLYNEKP IDGYLTIDFG EKLISTSEAQ AGFKVKLDFT
160 170 180 190 200
GWRAVGVSLN NDLENREMTL NATNTSSDGT QDSIGRSLGA KVDSIRFKAP
210 220 230 240 250
SNVSQGEIYI DRIMFSVDDA RYQWSDYQVK TRLSEPEIQF HNVKPQLPVT
260 270 280 290 300
PENLAAIDLI RQRLINEFVG GEKETNLALE ENISKLKSDF DALNIHTLAN
310 320 330 340 350
GGTQGRHLIT DKQIIIYQPE NLNSQDKQLF DNYVILGNYT TLMFNISRAY
360 370 380 390 400
VLEKDPTQKA QLKQMYLLMT KHLLDQGFVK GSALVTTHHW GYSSRWWYIS
410 420 430 440 450
TLLMSDALKE ANLQTQVYDS LLWYSREFKS SFDMKVSADS SDLDYFNTLS
460 470 480 490 500
RQHLALLLLE PDDQKRINLV NTFSHYITGA LTQVPPGGKD GLRPDGTAWR
510 520 530 540 550
HEGNYPGYSF PAFKNASQLI YLLRDTPFSV GESGWNNLKK AMVSAWIYSN
560 570 580 590 600
PEVGLPLAGR HPFNSPSLKS VAQGYYWLAM SAKSSPDKTL ASIYLAISDK
610 620 630 640 650
TQNESTAIFG ETITPASLPQ GFYAFNGGAF GIHRWQDKMV TLKAYNTNVW
660 670 680 690 700
SSEIYNKDNR YGRYQSHGVA QIVSNGSQLS QGYQQEGWDW NRMQGATTIH
710 720 730 740 750
LPLKDLDSPK PHTLMQRGER GFSGTSSLEG QYGMMAFDLI YPANLERFDP
760 770 780 790 800
NFTAKKSVLA ADNHLIFIGS NINSSDKNKN VETTLFQHAI TPTLNTLWIN
810 820 830 840 850
GQKIENMPYQ TTLQQGDWLI DSNGNGYLIT QAEKVNVSRQ HQVSAENKNR
860 870 880 890 900
QPTEGNFSSA WIDHSTRPKD ASYEYMVFLD ATPEKMGEMA QKFRENNGLY
910 920 930 940 950
QVLRKDKDVH IILDKLSNVT GYAFYQPASI EDKWIKKVNK PAIVMTHRQK
960 970 980 990 1000
DTLIVSAVTP DLNMTRQKAA TPVTINVTIN GKWQSADKNS EVKYQVSGDN
1010 1020
TELTFTSYFG IPQEIKLSPL P
Length:1,021
Mass (Da):115,092
Last modified:October 19, 2011 - v2
Checksum:i299406E6466568AC
GO

Sequence cautioni

The sequence described in PubMed:7512814 differs from that shown. Reason: Frameshift at positions 494 and 533.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti125L → P no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti369M → V no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti670A → G no nucleotide entry (PubMed:7512814).Curated1
Sequence conflicti865S → R no nucleotide entry (PubMed:7512814).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ996964 Genomic DNA. Translation: ACY01450.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GQ996964 Genomic DNA. Translation: ACY01450.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HN0X-ray1.90A1-1021[»]
SMRiP59807.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP59807. 2 interactors.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

Proteomic databases

PRIDEiP59807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15788.
BRENDAi4.2.2.20. 5049.

Miscellaneous databases

EvolutionaryTraceiP59807.

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
2.60.120.410. 1 hit.
2.60.220.10. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR008929. Chondroitin_lyas.
IPR024200. Chondroitinase_ABC_I.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR011071. Lyase_8-like_C.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
IPR015177. Lyase_catalyt.
IPR015176. Lyase_N.
[Graphical view]
PfamiPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF09093. Lyase_catalyt. 1 hit.
PF09092. Lyase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF034515. Chondroitinase. 1 hit.
SUPFAMiSSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCABC1_PROVU
AccessioniPrimary (citable) accession number: P59807
Secondary accession number(s): D0V0C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 19, 2011
Last modified: November 2, 2016
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

PubMed:7512814 shows amino acid differences at positions 317, 321, 410, 694, 738 and 866 due to incorrect translation of the nucleotide sequence.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.