UniProtKB - Q46079 (CSLB_PEDHD)

BLAST

>sp|Q46079|CSLB_PEDHD Chondroitinase-B OS=Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) OX=485917 GN=cslB PE=1 SV=2
MKMLNKLAGYLLPIMVLLNVAPCLGQVVASNETLYQVVKEVKPGGLVQIADGTYKDVQLI
VSNSGKSGLPITIKALNPGKVFFTGDAKVELRGEHLILEGIWFKDGNRAIQAWKSHGPGL
VAIYGSYNRITACVFDCFDEANSAYITTSLTEDGKVPQHCRIDHCSFTDKITFDQVINLN
NTARAIKDGSVGGPAMYHRVDHCFFSNPQKPGNAGGGIRIGYYRNDIGRCLVDSNLFMRQ
DSEAEIITSKSQENVYYGNTYLNCQGTMNFRHGDHQVAINNFYIGNDQRFGYGGMFVWGS
RHVIACNYFELSETIKSRGNAALYLNPGAMASEHALAFDMLIANNAFINVNGYAIHFNPL
DERRKEYCAANRLKFETPHQLMLKGNLFFKDKPYVYPFFKDDYFIAGKNSWTGNVALGVE
KGIPVNISANRSAYKPVKIKDIQPIEGIALDLNALISKGITGKPLSWDEVRPYWLKEMPG
TYALTARLSADRAAKFKAVIKRNKEH

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History
Entry version 101 (10 Oct 2018)
Sequence version 2 (03 Nov 2009)
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Protein

Chondroitinase-B

Gene

cslB

Organism

Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Cleaves the glycosaminoglycan, dermatan sulfate.

Catalytic activityⁱ

Eliminative cleavage of dermatan sulfate containing (1->4)-beta-D-hexosaminyl and (1->3)-beta-D-glucurosonyl or (1->3)-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (Delta-UA-GalNAc-4S).

Sites

Feature key	Position(s)	Length
Active siteⁱ	250	1
Active siteⁱ	272	1
Active siteⁱ	333	1

GO - Molecular functionⁱ

chondroitin B lyase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase

Molecular function

Lyase

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-15800 PHEP485917:G1GFH-804-MONOMER
BRENDAⁱ	4.2.2.19 2286
SABIO-RKⁱ	Q46079

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	PL6 Polysaccharide Lyase Family 6

CAZyⁱ

PL6 Polysaccharide Lyase Family 6

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Chondroitinase-B (EC:4.2.2.19) Alternative name(s): Chondroitin sulfate B lyase Chondroitin-B eliminase Chondroitin-B lyase
Gene namesⁱ	Name:cslB Ordered Locus Names:Phep_0789
Organismⁱ	Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Taxonomic identifierⁱ	485917 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › FCB group › Bacteroidetes/Chlorobi group › Bacteroidetes › Sphingobacteriia › Sphingobacteriales › Sphingobacteriaceae › Pedobacter › Pedobacter heparinus
Proteomesⁱ	UP000000852 Componentⁱ: Chromosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	250	K → A: Complete loss of activity. 1 Publication	1
Mutagenesisⁱ	272	H → A: Partial loss of activity. 1 Publication	1
Mutagenesisⁱ	333	E → A: Partial loss of activity. 1 Publication	1
Mutagenesisⁱ	363	R → A: No effect. 1 Publication	1
Mutagenesisⁱ	364	R → A: Partial loss of activity and altered product profile. 1 Publication	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04492 2-(Acetylamino)-2-Deoxy-4-O-Sulfo-Alpha-D-Galactopyranose DB03863 2-O-Methyl Fucose DB04548 4-Deoxy-D-Glucuronic Acid DB04515 6-Deoxy-2-O-Methyl-Alpha-L-Galactopyranose DB01872 Acetylgalactosamine-4-Sulfate DB03389 alpha-D-Xylopyranose DB02379 Beta-D-Glucose DB03088 Pyroglutamic Acid

DrugBankⁱ

DB04492 2-(Acetylamino)-2-Deoxy-4-O-Sulfo-Alpha-D-Galactopyranose
DB03863 2-O-Methyl Fucose
DB04548 4-Deoxy-D-Glucuronic Acid
DB04515 6-Deoxy-2-O-Methyl-Alpha-L-Galactopyranose
DB01872 Acetylgalactosamine-4-Sulfate
DB03389 alpha-D-Xylopyranose
DB02379 Beta-D-Glucose
DB03088 Pyroglutamic Acid

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 25	Add BLAST		25
ChainⁱPRO_0000024928	26 – 506	Chondroitinase-BAdd BLAST		481

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	26	Pyrrolidone carboxylic acid1 Publication		1
Glycosylationⁱ	234	O-linked (Man...) serine		1

Keywords - PTMⁱ

Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEⁱ	Q46079

PRIDEⁱ

Q46079

Interactionⁱ

Subunit structureⁱ

Monomer.

Protein-protein interaction databases

STRINGⁱ	485917.Phep_0789

STRINGⁱ

485917.Phep_0789

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	31 – 40	Combined sources	10
Beta strandⁱ	46 – 49	Combined sources	4
Beta strandⁱ	51 – 55	Combined sources	5
Beta strandⁱ	58 – 61	Combined sources	4
Beta strandⁱ	71 – 77	Combined sources	7
Beta strandⁱ	80 – 86	Combined sources	7
Beta strandⁱ	88 – 91	Combined sources	4
Beta strandⁱ	93 – 100	Combined sources	8
Beta strandⁱ	102 – 106	Combined sources	5
Turnⁱ	110 – 112	Combined sources	3
Beta strandⁱ	120 – 123	Combined sources	4
Beta strandⁱ	125 – 127	Combined sources	3
Beta strandⁱ	129 – 132	Combined sources	4
Beta strandⁱ	134 – 137	Combined sources	4
Beta strandⁱ	145 – 148	Combined sources	4
Beta strandⁱ	161 – 164	Combined sources	4
Beta strandⁱ	166 – 168	Combined sources	3
Beta strandⁱ	172 – 174	Combined sources	3
Beta strandⁱ	176 – 179	Combined sources	4
Beta strandⁱ	199 – 202	Combined sources	4
Beta strandⁱ	204 – 207	Combined sources	4
Beta strandⁱ	211 – 213	Combined sources	3
Beta strandⁱ	217 – 220	Combined sources	4
Beta strandⁱ	231 – 234	Combined sources	4
Beta strandⁱ	236 – 240	Combined sources	5
Beta strandⁱ	242 – 253	Combined sources	12
Beta strandⁱ	255 – 258	Combined sources	4
Beta strandⁱ	260 – 263	Combined sources	4
Beta strandⁱ	265 – 272	Combined sources	8
Beta strandⁱ	277 – 280	Combined sources	4
Beta strandⁱ	282 – 285	Combined sources	4
Beta strandⁱ	287 – 290	Combined sources	4
Beta strandⁱ	295 – 297	Combined sources	3
Beta strandⁱ	299 – 301	Combined sources	3
Beta strandⁱ	303 – 306	Combined sources	4
Beta strandⁱ	308 – 314	Combined sources	7
Turnⁱ	316 – 319	Combined sources	4
Beta strandⁱ	320 – 325	Combined sources	6
Beta strandⁱ	338 – 344	Combined sources	7
Beta strandⁱ	346 – 349	Combined sources	4
Beta strandⁱ	351 – 358	Combined sources	8
Helixⁱ	361 – 370	Combined sources	10
Beta strandⁱ	380 – 385	Combined sources	6
Beta strandⁱ	387 – 389	Combined sources	3
Beta strandⁱ	398 – 400	Combined sources	3
Beta strandⁱ	408 – 413	Combined sources	6
Beta strandⁱ	415 – 419	Combined sources	5
Beta strandⁱ	422 – 424	Combined sources	3
Helixⁱ	431 – 433	Combined sources	3
Helixⁱ	452 – 458	Combined sources	7
Helixⁱ	467 – 469	Combined sources	3
Helixⁱ	482 – 485	Combined sources	4
Helixⁱ	490 – 502	Combined sources	13

Show more details

3D structure databases

SMRⁱ	Q46079
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q46079

EvolutionaryTraceⁱ

Q46079

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K19053
OMAⁱ	RNDIGRC
Database of Orthologous Groups More...OrthoDBⁱ	POG091H03H8

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd14251 PL-6, 1 hit
Gene3Dⁱ	2.160.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence IPR039513 PL-6
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF14592 Chondroitinas_B, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q46079-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MKMLNKLAGY LLPIMVLLNV APCLGQVVAS NETLYQVVKE VKPGGLVQIA 
        60         70         80         90        100
DGTYKDVQLI VSNSGKSGLP ITIKALNPGK VFFTGDAKVE LRGEHLILEG 
       110        120        130        140        150
IWFKDGNRAI QAWKSHGPGL VAIYGSYNRI TACVFDCFDE ANSAYITTSL 
       160        170        180        190        200
TEDGKVPQHC RIDHCSFTDK ITFDQVINLN NTARAIKDGS VGGPAMYHRV 
       210        220        230        240        250
DHCFFSNPQK PGNAGGGIRI GYYRNDIGRC LVDSNLFMRQ DSEAEIITSK 
       260        270        280        290        300
SQENVYYGNT YLNCQGTMNF RHGDHQVAIN NFYIGNDQRF GYGGMFVWGS 
       310        320        330        340        350
RHVIACNYFE LSETIKSRGN AALYLNPGAM ASEHALAFDM LIANNAFINV 
       360        370        380        390        400
NGYAIHFNPL DERRKEYCAA NRLKFETPHQ LMLKGNLFFK DKPYVYPFFK 
       410        420        430        440        450
DDYFIAGKNS WTGNVALGVE KGIPVNISAN RSAYKPVKIK DIQPIEGIAL 
       460        470        480        490        500
DLNALISKGI TGKPLSWDEV RPYWLKEMPG TYALTARLSA DRAAKFKAVI 

KRNKEH

Length:506

Mass (Da):56,337

Last modified:November 3, 2009 - v2

Checksum:ⁱ454B93EC0AACD2A3

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	195	A → G in AAC83384 (PubMed:10618199).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U27584 Genomic DNA Translation: AAC83384.1 CP001681 Genomic DNA Translation: ACU03011.1
NCBI Reference Sequences More...RefSeqⁱ	WP_012780957.1, NZ_AQGK01000003.1

Genome annotation databases

EnsemblBacteriaⁱ	ACU03011; ACU03011; Phep_0789
KEGGⁱ	phe:Phep_0789

Similar proteinsⁱ

50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q46079	Uncharacterized protein		PSESL		512	UniRef50_Q46079
Chloramphenicol resistance protein		Marinifilum sp. JC075		525
UPI00000BB32D		PEDHE		506
UPI000377AE08		Pedobacter arcticus		489
UPI0000683342		PEDHE		481

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U27584 Genomic DNA Translation: AAC83384.1 CP001681 Genomic DNA Translation: ACU03011.1
RefSeqⁱ	WP_012780957.1, NZ_AQGK01000003.1

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DBG	X-ray	1.70	A	1-506	[»]
	1DBO	X-ray	1.70	A	1-506	[»]
	1OFL	X-ray	1.70	A	27-506	[»]
	1OFM	X-ray	1.80	A	27-506	[»]
SMRⁱ	Q46079
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	485917.Phep_0789

STRINGⁱ

485917.Phep_0789

Chemistry databases

DrugBankⁱ	DB04492 2-(Acetylamino)-2-Deoxy-4-O-Sulfo-Alpha-D-Galactopyranose DB03863 2-O-Methyl Fucose DB04548 4-Deoxy-D-Glucuronic Acid DB04515 6-Deoxy-2-O-Methyl-Alpha-L-Galactopyranose DB01872 Acetylgalactosamine-4-Sulfate DB03389 alpha-D-Xylopyranose DB02379 Beta-D-Glucose DB03088 Pyroglutamic Acid

DrugBankⁱ

Protein family/group databases

CAZyⁱ	PL6 Polysaccharide Lyase Family 6

CAZyⁱ

PL6 Polysaccharide Lyase Family 6

Proteomic databases

PRIDEⁱ	Q46079

PRIDEⁱ

Q46079

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ACU03011; ACU03011; Phep_0789
KEGGⁱ	phe:Phep_0789

Phylogenomic databases

KOⁱ	K19053
OMAⁱ	RNDIGRC
OrthoDBⁱ	POG091H03H8

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-15800 PHEP485917:G1GFH-804-MONOMER
BRENDAⁱ	4.2.2.19 2286
SABIO-RKⁱ	Q46079

Miscellaneous databases

EvolutionaryTraceⁱ	Q46079

EvolutionaryTraceⁱ

Q46079

Family and domain databases

CDDⁱ	cd14251 PL-6, 1 hit
Gene3Dⁱ	2.160.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence IPR039513 PL-6
Pfamⁱ	View protein in Pfam PF14592 Chondroitinas_B, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CSLB_PEDHD
Accessionⁱ	Q46079Primary (citable) accession number: Q46079 Secondary accession number(s): C6Y218
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
	Last sequence update:	November 3, 2009
	Last modified:	October 10, 2018
	This is version 101 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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Proteomes

Annotation systems

Supporting data

UniProtKB - Q46079 (CSLB_PEDHD)

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Chondroitinase-B

cslB

Select a section on the left to see content.

<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

Sites

<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

Enzyme and pathway databases

Protein family/group databases

<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 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

Chemistry databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

<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

<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

3D structure databases

Miscellaneous databases

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ