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Entry version 37 (11 Dec 2019)
Sequence version 2 (31 Oct 2012)
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Protein

Chondroitin sulfate ABC exolyase

Gene

chonabc

Organism
Bacteroides thetaiotaomicron
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 degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against acharan sulfate, heparin or heparan sulfate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • 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 EC:4.2.2.21

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+2 Publications, Mg2+2 PublicationsNote: Divalent metal cation. Requires divalent metal cation for binding of dermatan sulfate substrate, whereas it is not necessary for the binding of chondroitin sulfate substrates. Prefers Ca2+ or Mg2+, binding 1 ion per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Specific activity for chondroitin sulfate substrates increases moderately (2-fold) while an increase of 25-fold is observed for dermatan sulfate as substrate upon addition of Ca2+ or Mg2+ ions (PubMed:18227125). Increasing the concentration of Na+, K+ or Cs+ chloride from 0 to 0.1 M, increases the activity against all substrates. Further increases in salt concentration reduces the activity dramatically, with 50% inhibition occurring at 0.15 M and nearly complete inhibition at 0.4 M salt. The addition of 10 mM Ca2+ or Mg2+ ions increases the activity against chondroitin 4- and 6-sulfates by 2-3-fold, while the activity against dermatan sulfate increases much more significantly by 50-fold (PubMed:18512954). Addition of Mn2+ and Zn2+ reduces activity against chondroitin sulfate substrates, but increases the activity against dermatan sulfate. Increasing the concentration of CaCl2 with both chondroitin 4- and 6-sulfates from 0 to 0.04 M increases the activity. A further increase reduces activity, with 50% inhibition at 0.065-0.085 M and a complete inhibition of the reaction at 0.2 M. In case of dermatan sulfate, the addition of low concentration of CaCl2 dramatically increases the activity from the basal level. The maximal activity is reached at 0.01 M CaCl2.2 Publications

<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

Kcat is 15792 min(-1) with chondroitin 4-sulfate from porcine or bovine trachea as substrate. Kcat is 10404 min(-1) with chondroitin 6-sulfate from shark cartilage as substrate. Kcat is 2307 min(-1) with dermatan sulfate from porcine intestinal mucosa as substrate.2 Publications
  1. KM=67 µM for chondroitin 4-sulfate from porcine or bovine trachea (at 37 degrees Celsius and pH 7.6)2 Publications
  2. KM=33 µM for chondroitin 6-sulfate from shark cartilage (at 37 degrees Celsius and pH 7.6)2 Publications
  3. KM=61 µM for dermatan sulfate from porcine intestinal mucosa (at 37 degrees Celsius and pH 7.6)2 Publications
  1. Vmax=77.6 µmol/min/mg enzyme with chondroitin 4-sulfate from bovine trachea as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6)2 Publications
  2. Vmax=47.4 µmol/min/mg enzyme with chondroitin 6-sulfate from shark cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6)2 Publications
  3. Vmax=14.4 µmol/min/mg enzyme with chondroitin 2,6-sulfate from skate cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6)2 Publications
  4. Vmax=28.5 µmol/min/mg enzyme with chondroitin 4,6-sulfate from squid cartilage as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6)2 Publications
  5. Vmax=9.1 µmol/min/mg enzyme with dermatan sulfate from porcine intestinal mucosa as substrate (at 37 degrees Celsius and in 50 mM phosphate at pH 7.6)2 Publications

pH dependencei

Optimum pH is 7.6. Decreased activity at pH values below 7.0 and above 8.0. The activity against chondroitin 6-sulfate remains higher than with other substrates at low pH. At pH 6.5 the enzyme exhibits almost 60% of its maximal activity against chondroitin 6-sulfate, only 20% activity against chondroitin 4-sulfate and no measurable activity against dermatan sulfate. In contrast, at pH of 8.5 about 30% of enzyme's maximal activity against all substrates is displayed.2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius. No significant reduction in activity at temperatures in the range of 25-40 degrees Celsius. At 50 degrees Celsius, activity of 45% for dermatan sulfate, 60% for chondroitin 4-sulfate and 75% for chondroitin 6-sulfate is detected. Thermal denaturation curve is bimodal with two consecutive thermal denaturation midpoints (Tm) corresponding to 44 and 50 degrees Celsius, respectively.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi24Calcium1 Publication1
Metal bindingi26Calcium1 Publication1
Metal bindingi50Calcium; via carbonyl oxygen1 Publication1
Metal bindingi53Calcium; via carbonyl oxygen1 Publication1
Metal bindingi161Calcium1 Publication1
<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>Sitei172Important for catalytic activity against all substrates1 Publication1
Sitei344Important for catalytic activity against dermatan sulfate substrate2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei345Proton acceptor2 Publications1
Active sitei454Proton acceptor2 Publications1
Active sitei461Proton donor2 Publications1
Sitei514Transition state stabilizer1 Publication1
Sitei628Important for catalytic activity against all substrates2 Publications1

<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
LigandCalcium, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
C5G6D7

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
PL8 Polysaccharide Lyase Family 8

<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%5Fand%5Ftaxonomy%5Fsection">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 exolyase1 PublicationImported (EC:4.2.2.212 Publications)
Alternative name(s):
Chondroitin ABC exoeliminaseBy similarity
Chondroitin ABC lyase II1 PublicationBy similarity
Chondroitin sulfate ABC lyase II1 PublicationBy similarity
Short name:
ChS ABC lyase IIBy similarity
Chondroitinase ABC II1 PublicationBy similarity
Short name:
cABC IIBy similarity
Exochondroitinase ABCBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:chonabc
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBacteroides thetaiotaomicron
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri818 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

<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

Keywords - Cellular componenti

Periplasm

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi172R → A: Loss of activity against all substrates. 1 Publication1
Mutagenesisi173Q → A: Reduced activity against all substrates by a factor of about 2-10. 1 Publication1
Mutagenesisi267R → A: Reduced activity against all substrates by a factor of about 2-10. 1 Publication1
Mutagenesisi344H → A: No detectable activity against dermatan sulfate in the standard assay, but after overnight incubation shows traces of degradation products, also still degrades chondroitin sulfate albeit with 10- to 30-fold lower catalytic efficiency. 2 Publications1
Mutagenesisi344H → D or E: Loss of activity against all substrates. 2 Publications1
Mutagenesisi344H → N: Retains 5-25% catalytic efficiency against all substrates. 2 Publications1
Mutagenesisi344H → Q: Retains 5% catalytic efficiency against chondroitin 4-sulfate only. 2 Publications1
Mutagenesisi345H → A: No activity against dermatan sulfate even after overnight incubation, but still degrades chondroitin sulfate albeit with 10- to 30-fold lower catalytic efficiency. 2 Publications1
Mutagenesisi345H → D or E: Loss of activity against all substrates. 2 Publications1
Mutagenesisi345H → N or Q: Low levels of activity against chondroitin sulfate substrates, but no activity against dermatan sulfate. 2 Publications1
Mutagenesisi453H → A: Slightly reduced activity against all substrates. 2 Publications1
Mutagenesisi453H → N: Shows no activity against dermatan sulfate while retaining about 10% of its catalytic efficiency against chondroitin 4- and 6-sulfates. 2 Publications1
Mutagenesisi454H → A, D, N or Q: Loss of activity against all substrates. 2 Publications1
Mutagenesisi461Y → A: Loss of activity against all substrates. 2 Publications1
Mutagenesisi514R → A: Loss of activity against all substrates. 1 Publication1
Mutagenesisi628E → A or D: Loss of activity against all substrates. 2 Publications1
Mutagenesisi628E → Q: Retains low levels of activity against chondroitin sulfate substrates, but not against dermatan sulfate as substrate. 2 Publications1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 14Sequence analysisAdd BLAST14
<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_000042012315 – 1014Chondroitin sulfate ABC exolyaseSequence analysisAdd BLAST1000

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
C5G6D7

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

<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

Secondary structure

11014
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
C5G6D7

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105TCD Bacteria
ENOG410Y18H LUCA

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
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
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

C5G6D7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLILSFLCPA FLNAQIVTDE RMFSFEEPQL PACITGVQSQ LGISGAHYKD
60 70 80 90 100
GKHSLEWTFE PNGRLELRKD LKFEKKDPTG KDLYLSAFIV WIYNEQPQDA
110 120 130 140 150
AIEFEFLKDG RKCASFPFGI NFKGWRAAWV CYERDMQGTP EEGMNELRIV
160 170 180 190 200
APDAKGRLFI DHLITATKVD ARQQTADLQV PFVNAGTTNH WLVLYKHSLL
210 220 230 240 250
KPDIELTPVS DKQRQEMKLL EKRFRDMIYT KGKVTEKEAE TIRKKYDLYQ
260 270 280 290 300
ITYKDGQVSG VPVFMVRASE AYERMIPDWD KDMLTKMGIE MRAYFDLMKR
310 320 330 340 350
IAVAYNNSEA GSPIRKEMRR KFLAMYDHIT DQGVAYGSCW GNIHHYGYSV
360 370 380 390 400
RGLYPAYFLM KDVLREEGKL LEAERTLRWY AITNEVYPKP EGNGIDMDSF
410 420 430 440 450
NTQTTGRIAS ILMMEDTPEK LQYLKSFSRW IDYGCRPAPG LAGSFKVDGG
460 470 480 490 500
AFHHRNNYPA YAVGGLDGAT NMIYLFSRTS LAVSELAHRT VKDVLLAMRF
510 520 530 540 550
YCNKLNFPLS MSGRHPDGKG KLVPMHYAIM AIAGTPDGKG DFDKEMASAY
560 570 580 590 600
LRLVSSDSSS AEQAPEYMPK VSNAQERKIA KRLVENGFRA EPDPQGNLSL
610 620 630 640 650
GYGCVSVQRR ENWSAVARGH SRYLWAAEHY LGHNLYGRYL AHGSLQILTA
660 670 680 690 700
PPGQTVTPTT SGWQQEGFDW NRIPGVTSIH LPLDLLKANV LNVDTFSGME
710 720 730 740 750
EMLYSDEAFA GGLSQGKMNG NFGMKLHEHD KYNGTHRARK SFHFIDGMIV
760 770 780 790 800
CLGSDIENTN MDYPTETTIF QLAVTDKAAH DYWKNNAGEG KVWMDHLGTG
810 820 830 840 850
YYVPVAARFE KNFPQYSRMQ DTGKETKGDW VSLIIDHGKA PKAGSYEYAI
860 870 880 890 900
LPGTDRKTMT AFAKKPAYSV LQQDRNAHIL ESPSDRITSY VLFETPQSLL
910 920 930 940 950
PGGLLQRTDT SCLVMVRKES ADKVLLTVAQ PDLALYRGPS DEAFDKDGKR
960 970 980 990 1000
MERSIYSRPW IDNESGEIPV TVTLKGRWKV VETPYCKVVS EDKKQTVLRF
1010
LCKDGASYEV ELEK
Length:1,014
Mass (Da):114,921
Last modified:October 31, 2012 - v2
<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:i10C46B91CF02A44A
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence ABV21364 differs from that shown. Cloning artifact.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EF639172 Genomic DNA Translation: ABV21364.1 Sequence problems.

<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
EF639172 Genomic DNA Translation: ABV21364.1 Sequence problems.

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q1FX-ray2.85A/B1-1014[»]
SMRiC5G6D7
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

CAZyiPL8 Polysaccharide Lyase Family 8

Proteomic databases

PRIDEiC5G6D7

Phylogenomic databases

eggNOGiENOG4105TCD Bacteria
ENOG410Y18H LUCA

Enzyme and pathway databases

SABIO-RKiC5G6D7

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
IPR003159 Lyase_8_central_dom
IPR015177 Lyase_catalyt
IPR015176 Lyase_N
PANTHERiPTHR37322 PTHR37322, 1 hit
PfamiView protein in Pfam
PF02278 Lyase_8, 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_BACT4
<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: C5G6D7
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: October 31, 2012
Last modified: December 11, 2019
This is version 37 of the entry and version 2 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

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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