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Protein

Chondroitin sulfate ABC endolyase

Gene
N/A
Organism
Proteus vulgaris
Status
Reviewed-Annotation score: -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

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

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 Delta4-unsaturated oligosaccharides of different sizes that are ultimately degraded to Delta4-unsaturated tetra- and disaccharides.4 Publications

Activity 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

Keywordsi

Molecular functionLyase
Biological processCarbohydrate metabolism
LigandCalcium, 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

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
MINTiP59807

Structurei

Secondary structure

11021
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
2.60.220.10, 1 hit
2.70.98.10, 1 hit
InterProiView protein in InterPro
IPR039174 Chondroitin_ABC_lyase
IPR008929 Chondroitin_lyas
IPR024200 Chondroitinase_ABC_I
IPR011013 Gal_mutarotase_sf_dom
IPR008979 Galactose-bd-like_sf
IPR014718 GH-type_carb-bd
IPR011071 Lyase_8-like_C
IPR004103 Lyase_8_C
IPR003159 Lyase_8_central_dom
IPR015177 Lyase_catalyt
IPR015176 Lyase_N
PANTHERiPTHR37322 PTHR37322, 1 hit
PfamiView protein in Pfam
PF02278 Lyase_8, 1 hit
PF02884 Lyase_8_C, 1 hit
PF09093 Lyase_catalyt, 1 hit
PF09092 Lyase_N, 1 hit
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

Similar proteinsi

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
MINTiP59807

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
2.60.220.10, 1 hit
2.70.98.10, 1 hit
InterProiView protein in InterPro
IPR039174 Chondroitin_ABC_lyase
IPR008929 Chondroitin_lyas
IPR024200 Chondroitinase_ABC_I
IPR011013 Gal_mutarotase_sf_dom
IPR008979 Galactose-bd-like_sf
IPR014718 GH-type_carb-bd
IPR011071 Lyase_8-like_C
IPR004103 Lyase_8_C
IPR003159 Lyase_8_central_dom
IPR015177 Lyase_catalyt
IPR015176 Lyase_N
PANTHERiPTHR37322 PTHR37322, 1 hit
PfamiView protein in Pfam
PF02278 Lyase_8, 1 hit
PF02884 Lyase_8_C, 1 hit
PF09093 Lyase_catalyt, 1 hit
PF09092 Lyase_N, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: October 19, 2011
Last modified: September 12, 2018
This is version 79 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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