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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Sodium or calcium; via carbonyl oxygen
Metal bindingi70 – 701Sodium or calcium; via carbonyl oxygen
Metal bindingi73 – 731Sodium or calcium; via carbonyl oxygen
Metal bindingi211 – 2111Sodium or calcium
Active sitei501 – 5011Proton acceptor2 Publications
Active sitei508 – 5081Proton donorSequence analysis
Sitei560 – 5601Transition state stabilizerSequence analysis
Sitei653 – 6531Important for catalytic activity

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi500 – 5001R → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with highly reduced catalytic efficiency. 2 Publications
Mutagenesisi501 – 5011H → A, K or R: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications
Mutagenesisi508 – 5081Y → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications
Mutagenesisi508 – 5081Y → F: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with greatly reduced catalytic efficiency. 2 Publications
Mutagenesisi560 – 5601R → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications
Mutagenesisi561 – 5611H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication
Mutagenesisi653 – 6531E → A or D: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 2 Publications
Mutagenesisi653 – 6531E → Q: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 2 Publications
Mutagenesisi712 – 7121H → A: Still active on both chondroitin 6-sulfate and dermatan sulfate, but with reduced catalytic efficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 1021997Chondroitin sulfate ABC endolyasePRO_0000024929Add
BLAST

Expressioni

Inductioni

By chondroitin sulfate or its degraded products.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP59807. 2 interactions.

Structurei

Secondary structure

1
1021
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 423Combined sources
Beta strandi46 – 483Combined sources
Turni49 – 524Combined sources
Beta strandi59 – 679Combined sources
Beta strandi69 – 724Combined sources
Beta strandi74 – 807Combined sources
Beta strandi84 – 885Combined sources
Helixi96 – 1038Combined sources
Beta strandi105 – 11915Combined sources
Beta strandi122 – 13211Combined sources
Beta strandi140 – 1467Combined sources
Beta strandi151 – 1588Combined sources
Turni159 – 1613Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi204 – 21916Combined sources
Helixi251 – 26919Combined sources
Helixi283 – 2919Combined sources
Helixi313 – 3175Combined sources
Helixi319 – 3213Combined sources
Helixi324 – 3307Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 35217Combined sources
Helixi356 – 37520Combined sources
Helixi390 – 40314Combined sources
Helixi405 – 4106Combined sources
Helixi414 – 42411Combined sources
Helixi425 – 4284Combined sources
Helixi429 – 4324Combined sources
Turni438 – 4414Combined sources
Helixi443 – 4486Combined sources
Helixi450 – 4589Combined sources
Helixi463 – 48220Combined sources
Beta strandi490 – 4923Combined sources
Beta strandi498 – 5003Combined sources
Helixi506 – 52318Combined sources
Helixi532 – 54716Combined sources
Beta strandi549 – 5535Combined sources
Helixi555 – 5573Combined sources
Helixi568 – 5714Combined sources
Helixi572 – 5798Combined sources
Helixi588 – 59811Combined sources
Helixi602 – 6098Combined sources
Beta strandi621 – 6255Combined sources
Helixi626 – 6283Combined sources
Beta strandi630 – 6356Combined sources
Beta strandi638 – 6436Combined sources
Beta strandi649 – 6513Combined sources
Helixi662 – 6643Combined sources
Beta strandi667 – 67610Combined sources
Helixi679 – 6813Combined sources
Beta strandi697 – 6993Combined sources
Helixi703 – 7064Combined sources
Beta strandi709 – 7124Combined sources
Beta strandi719 – 7213Combined sources
Beta strandi724 – 7285Combined sources
Turni729 – 7313Combined sources
Beta strandi732 – 7409Combined sources
Beta strandi753 – 7619Combined sources
Beta strandi764 – 77310Combined sources
Turni775 – 7806Combined sources
Beta strandi781 – 7899Combined sources
Beta strandi792 – 7943Combined sources
Beta strandi797 – 7993Combined sources
Beta strandi802 – 8043Combined sources
Beta strandi807 – 8137Combined sources
Beta strandi818 – 8203Combined sources
Beta strandi826 – 8316Combined sources
Beta strandi835 – 84511Combined sources
Turni847 – 8493Combined sources
Beta strandi852 – 86312Combined sources
Helixi864 – 8663Combined sources
Beta strandi867 – 87812Combined sources
Helixi883 – 89412Combined sources
Beta strandi898 – 91417Combined sources
Turni915 – 9184Combined sources
Beta strandi919 – 9268Combined sources
Beta strandi933 – 94816Combined sources
Beta strandi953 – 9586Combined sources
Beta strandi966 – 9683Combined sources
Beta strandi973 – 9819Combined sources
Beta strandi983 – 9864Combined sources
Beta strandi993 – 9975Combined sources
Beta strandi1000 – 10089Combined sources
Beta strandi1013 – 10197Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HN0X-ray1.90A1-1021[»]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti125 – 1251L → P no nucleotide entry (PubMed:7512814).Curated
Sequence conflicti369 – 3691M → V no nucleotide entry (PubMed:7512814).Curated
Sequence conflicti670 – 6701A → G no nucleotide entry (PubMed:7512814).Curated
Sequence conflicti865 – 8651S → R no nucleotide entry (PubMed:7512814).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1HN0X-ray1.90A1-1021[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP59807. 2 interactions.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

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...

Publicationsi

  1. "Cloning and expression in Escherichia coli of the gene encoding the Proteus vulgaris chondroitin ABC lyase."
    Sato N., Shimada M., Nakajima H., Oda H., Kimura S.
    Appl. Microbiol. Biotechnol. 41:39-46(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-42, CATALYTIC ACTIVITY, INDUCTION.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  2. "Cloning and expression of the chondroitinase I and II genes from Proteus vulgaris."
    Ryan M.J., Khandke K.M., Tilley B.C., Lotvin J.A.
    Patent number WO9425567, 10-NOV-1994
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Use of chondroitin sulfate lyases in combination for promotion of neurite growth."
    Tam K.W., Wang Q., Li R.A., Chan Y.S., Shum D.K.Y.
    Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-1021.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  4. "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides."
    Hamai A., Hashimoto N., Mochizuki H., Kato F., Makiguchi Y., Horie K., Suzuki S.
    J. Biol. Chem. 272:9123-9130(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  5. "Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification."
    Prabhakar V., Capila I., Bosques C.J., Pojasek K., Sasisekharan R.
    Biochem. J. 386:103-112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE RESIDUES, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-500; HIS-501; TYR-508; ARG-560; HIS-561; GLU-653 AND HIS-712.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  6. "Biochemical characterization of the chondroitinase ABC I active site."
    Prabhakar V., Raman R., Capila I., Bosques C.J., Pojasek K., Sasisekharan R.
    Biochem. J. 390:395-405(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ACTIVE SITE RESIDUES, MUTAGENESIS OF ARG-500; HIS-501; TYR-508; ARG-560 AND GLU-653.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  7. "How does chondroitinase promote functional recovery in the damaged CNS?"
    Crespo D., Asher R.A., Lin R., Rhodes K.E., Fawcett J.W.
    Exp. Neurol. 206:159-171(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN DAMAGED CNS RECOVERY.
  8. "Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution."
    Huang W., Lunin V.V., Li Y., Suzuki S., Sugiura N., Miyazono H., Cygler M.
    J. Mol. Biol. 328:623-634(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SODIUM ION, DOMAIN, DISCUSSION OF SEQUENCE.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.

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: July 6, 2016
This is version 70 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.