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Entry version 31 (11 Dec 2019)
Sequence version 1 (13 Oct 2009)
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Protein

Chondroitin sulfate ABC exolyase

Gene

ChABCII

Organism
Proteus vulgaris
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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). Optimum temperature is 37 degrees Celsius (PubMed:18849565).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei453Proton acceptor1 Publication1
Active sitei460Proton donorSequence analysis1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei513Transition state stabilizerSequence analysis1
Sitei608Important for catalytic activity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processCarbohydrate metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15789

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ChABCII
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiProteus vulgaris
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri585 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi343H → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1
Mutagenesisi452H → A: Slight decrease in substrate affinity, but greatly reduced (100-fold) catalytic efficiency. 1 Publication1
Mutagenesisi453H → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1
Mutagenesisi456H → A: 3-fold decrease in catalytic efficiency with both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1
Mutagenesisi460Y → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1
Mutagenesisi513R → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1
Mutagenesisi608E → A: Loss of activity on both chondroitin 6-sulfate and dermatan sulfate. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000413627‹1 – 990Chondroitin sulfate ABC exolyaseAdd BLAST›990

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
585.DR95_2845

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
C7S340

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.50.10.100, 1 hit
2.60.220.10, 1 hit
2.70.98.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

The PANTHER Classification System

More...
PANTHERi
PTHR37322 PTHR37322, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02278 Lyase_8, 1 hit
PF02884 Lyase_8_C, 1 hit
PF09093 Lyase_catalyt, 1 hit
PF09092 Lyase_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF034515 Chondroitinase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48230 SSF48230, 1 hit
SSF49785 SSF49785, 1 hit
SSF49863 SSF49863, 1 hit
SSF74650 SSF74650, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7AA786306AAADF08
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EF988659 Genomic DNA Translation: ABU46331.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

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

3D structure databases

SMRiC7S340
ModBaseiSearch...

Protein-protein interaction databases

STRINGi585.DR95_2845

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15789

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCABC2_PROVU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C7S340
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 13, 2009
Last modified: December 11, 2019
This is version 31 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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