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Protein

Chondroitin sulfate ABC exolyase

Gene

ChABCII

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

Functioni

Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the respective disaccharides. To a lesser extent, is also able to split off disaccharide residues directly from polymeric chondroitin 4- and 6-sulfate, dermatan sulfate, chondroitin, and hyaluronan. Is not active against keratan sulfate, heparan sulfate, and heparin.2 Publications

Catalytic activityi

Exolytic removal of Delta(4)-unsaturated disaccharide residues from the non-reducing ends of both polymeric chondroitin/dermatan sulfates and their oligosaccharide fragments.2 Publications

Enzyme regulationi

Inhibited by Zn2+, whereas Ni2+, Fe2+, and Cu2+ have little or no effect on activity.1 Publication

Kineticsi

  1. KM=33 µM for chondroitin 6-sulfate tetrasaccharide2 Publications
  2. KM=80 µM for chondroitin 6-sulfate2 Publications
  3. KM=9.8 µM for chondroitin 6-sulfate2 Publications
  4. KM=16.1 µM for chondroitin 4-sulfate2 Publications
  5. KM=19.2 µM for dermatan sulfate2 Publications
  1. Vmax=155 µmol/min/mg enzyme with chondroitin 6-sulfate tetrasaccharide as substrate2 Publications
  2. Vmax=34 µmol/min/mg enzyme with chondroitin 6-sulfate as substrate2 Publications

pH dependencei

Optimum pH is 8.2 Publications

Temperature dependencei

Optimum temperature is 40 degrees Celsius (PubMed:9083041) or 37 degrees Celsius (PubMed:18849565).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei453 – 4531Proton acceptor1 Publication
Active sitei460 – 4601Proton donorSequence analysis
Sitei513 – 5131Transition state stabilizerSequence analysis
Sitei608 – 6081Important for catalytic activity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15789.

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin sulfate ABC exolyase (EC:4.2.2.21)
Alternative name(s):
Chondroitin ABC exoeliminase
Chondroitin ABC lyase II
Chondroitin sulfate ABC lyase II
Short name:
ChS ABC lyase II
Chondroitinase ABC II
Short name:
cABC II
Exochondroitinase ABC
Gene namesi
Name:ChABCII
OrganismiProteus vulgaris
Taxonomic identifieri585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi343 – 3431H → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication
Mutagenesisi452 – 4521H → A: Slight decrease in substrate affinity, but greatly reduced (100-fold) catalytic efficiency. 1 Publication
Mutagenesisi453 – 4531H → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication
Mutagenesisi456 – 4561H → A: 3-fold decrease in catalytic efficiency with both chondroitin 6-sulfate and dermatan sulfate. 1 Publication
Mutagenesisi460 – 4601Y → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication
Mutagenesisi513 – 5131R → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication
Mutagenesisi608 – 6081E → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 990›990Chondroitin sulfate ABC exolyasePRO_0000413627Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

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. Glyco_hydro-type_carb-bd_sub.
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: Fragment.

C7S340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LPTLSHEAFG DIYLFEGELP NTLTTSNNNQ LSLSKQHAKD GEQSLKWQYQ
60 70 80 90 100
PQATLTLNNI VNYQDDKNTA TPLTFMMWIY NEKPQSSPLT LAFKQNNKIA
110 120 130 140 150
LSFNAELNFT GWRGIAVPFR DMQGSATGQL DQLVITAPNQ AGTLFFDQII
160 170 180 190 200
MSVPLDNRWA VPDYQTPYVN NAVNTMVSKN WSALLMYDQM FQAHYPTLNF
210 220 230 240 250
DTEFRDDQTE MASIYQRFEY YQGIRSDKKI TPDMLDKHLA LWEKLVLTQH
260 270 280 290 300
ADGSITGKAL DHPNRQHFMK VEGVFSEGTQ KALLDANMLR DVGKTLLQTA
310 320 330 340 350
IYLRSDSLSA TDRKKLEERY LLGTRYVLEQ GFTRGSGYQI ITHVGYQTRE
360 370 380 390 400
LFDAWFIGRH VLAKNNLLAP TQQAMMWYNA TGRIFEKNNE IVDANVDILN
410 420 430 440 450
TQLQWMIKSL LMLPDYQQRQ QALAQLQSWL NKTILSSKGV AGGFKSDGSI
460 470 480 490 500
FHHSQHYPAY AKDAFGGLAP SVYALSDSPF RLSTSAHERL KDVLLKMRIY
510 520 530 540 550
TKETQIPVVL SGRHPTGLHK IGIAPFKWMA LAGTPDGKQK LDTTLSAAYA
560 570 580 590 600
KLDNKTHFEG INAESEPVGA WAMNYASMAI QRRASTQSPQ QSWLAIARGF
610 620 630 640 650
SRYLVGNESY ENNNRYGRYL QYGQLEIIPA DLTQSGFSHA GWDWNRYPGT
660 670 680 690 700
TTIHLPYNEL EAKLNQLPAA GIEEMLLSTE SYSGANTLNN NSMFAMKLHG
710 720 730 740 750
HSKYQQQSLR ANKSYFLFDN RVIALGSGIE NDDKQHTTET TLFQFAVPKL
760 770 780 790 800
QSVIINGKKV NQLDTQLTLN NADTLIDPTG NLYKLTKGQT VKFSYQKQHS
810 820 830 840 850
LDDRNSKPTE QLFATAVISH GKAPSNENYE YAIAIEAQNN KAPEYTVLQH
860 870 880 890 900
NDQLHAVKDK ITQEEGYAFF EATKLKSADA TLLSSDAPVM VMAKIQNQQL
910 920 930 940 950
TLSIVNPDLN LYQGREKDQF DDKGNQIEVS VYSRHWLTAE SQSTNSTITV
960 970 980 990
KGIWKLTTPQ PGVIIKHHNN NTLITTTTIQ ATPTVINLVK
Length:990
Mass (Da):111,744
Last modified:October 13, 2009 - v1
Checksum:i7AA786306AAADF08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF988659 Genomic DNA. Translation: ABU46331.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF988659 Genomic DNA. Translation: ABU46331.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15789.

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. Glyco_hydro-type_carb-bd_sub.
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, recombinant expression, characterization and mutagenesis of chondroitin sulphate ABC exolyase from Proteus vulgaris."
    Tam K.-W., Wang Q., Li R.A., Chan Y.-S., Shum D.K.-Y.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.
  2. "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.
  3. "Recombinant expression, purification, and biochemical characterization of chondroitinase ABC II from Proteus vulgaris."
    Prabhakar V., Capila I., Soundararajan V., Raman R., Sasisekharan R.
    J. Biol. Chem. 284:974-982(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE RESIDUES, MUTAGENESIS OF HIS-343; HIS-452; HIS-453; HIS-456; TYR-460; ARG-513 AND GLU-608.
    Strain: ATCC 6896 / NBRC 3988 / NCIMB 8065 / NCTC 4636.

Entry informationi

Entry nameiCABC2_PROVU
AccessioniPrimary (citable) accession number: C7S340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 13, 2009
Last modified: October 29, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.