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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: Annotation score: 5 out of 5-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei250 – 2501
Active sitei272 – 2721
Active sitei333 – 3331

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15800.
PHEP485917:GHL9-795-MONOMER.
BRENDAi4.2.2.19. 2286.
SABIO-RKQ46079.

Protein family/group databases

CAZyiPL6. 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
OrganismiPedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Taxonomic identifieri485917 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter
Proteomesi
  • UP000000852 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501K → A: Complete loss of activity. 1 Publication
Mutagenesisi272 – 2721H → A: Partial loss of activity. 1 Publication
Mutagenesisi333 – 3331E → A: Partial loss of activity. 1 Publication
Mutagenesisi363 – 3631R → A: No effect. 1 Publication
Mutagenesisi364 – 3641R → A: Partial loss of activity and altered product profile. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Chaini26 – 506481Chondroitinase-BPRO_0000024928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Pyrrolidone carboxylic acid
Glycosylationi234 – 2341O-linked (Man...)

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi485917.Phep_0789.

Structurei

Secondary structure

1
506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4010Combined sources
Beta strandi46 – 494Combined sources
Beta strandi51 – 555Combined sources
Beta strandi58 – 614Combined sources
Beta strandi71 – 777Combined sources
Beta strandi80 – 867Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi102 – 1065Combined sources
Turni110 – 1123Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi242 – 25312Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi260 – 2634Combined sources
Beta strandi265 – 2728Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi287 – 2904Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi299 – 3013Combined sources
Beta strandi303 – 3064Combined sources
Beta strandi308 – 3147Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 3256Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi351 – 3588Combined sources
Helixi361 – 37010Combined sources
Beta strandi380 – 3856Combined sources
Beta strandi387 – 3893Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi408 – 4136Combined sources
Beta strandi415 – 4195Combined sources
Beta strandi422 – 4243Combined sources
Helixi431 – 4333Combined sources
Helixi452 – 4587Combined sources
Helixi467 – 4693Combined sources
Helixi482 – 4854Combined sources
Helixi490 – 50213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DBGX-ray1.70A1-506[»]
1DBOX-ray1.70A1-506[»]
1OFLX-ray1.70A27-506[»]
1OFMX-ray1.80A27-506[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46079.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK19053.
OMAiRNDIGRC.
OrthoDBiPOG091H03H8.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q46079-1 [UniParc]FASTAAdd to basket

« Hide

        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
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951A → G in AAC83384 (PubMed:10618199).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27584 Genomic DNA. Translation: AAC83384.1.
CP001681 Genomic DNA. Translation: ACU03011.1.
RefSeqiWP_012780957.1. NZ_AQGK01000003.1.

Genome annotation databases

EnsemblBacteriaiACU03011; ACU03011; Phep_0789.
KEGGiphe:Phep_0789.
PATRICi22878621. VBIPedHep98714_0806.

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.
RefSeqiWP_012780957.1. NZ_AQGK01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DBGX-ray1.70A1-506[»]
1DBOX-ray1.70A1-506[»]
1OFLX-ray1.70A27-506[»]
1OFMX-ray1.80A27-506[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi485917.Phep_0789.

Protein family/group databases

CAZyiPL6. Polysaccharide Lyase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACU03011; ACU03011; Phep_0789.
KEGGiphe:Phep_0789.
PATRICi22878621. VBIPedHep98714_0806.

Phylogenomic databases

KOiK19053.
OMAiRNDIGRC.
OrthoDBiPOG091H03H8.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15800.
PHEP485917:GHL9-795-MONOMER.
BRENDAi4.2.2.19. 2286.
SABIO-RKQ46079.

Miscellaneous databases

EvolutionaryTraceiQ46079.

Family and domain databases

Gene3Di2.160.20.10. 1 hit.
InterProiIPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
SUPFAMiSSF51126. SSF51126. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCSLB_PEDHD
AccessioniPrimary (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: September 7, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.