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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)DescriptionActionsGraphical viewLength
Active sitei2501
Active sitei2721
Active sitei3331

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15800.
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)DescriptionActionsGraphical viewLength
Mutagenesisi250K → A: Complete loss of activity. 1 Publication1
Mutagenesisi272H → A: Partial loss of activity. 1 Publication1
Mutagenesisi333E → A: Partial loss of activity. 1 Publication1
Mutagenesisi363R → A: No effect. 1 Publication1
Mutagenesisi364R → A: Partial loss of activity and altered product profile. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
ChainiPRO_000002492826 – 506Chondroitinase-BAdd BLAST481

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26Pyrrolidone carboxylic acid1
Glycosylationi234O-linked (Man...)1

Keywords - PTMi

Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi485917.Phep_0789.

Structurei

Secondary structure

1506
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 40Combined sources10
Beta strandi46 – 49Combined sources4
Beta strandi51 – 55Combined sources5
Beta strandi58 – 61Combined sources4
Beta strandi71 – 77Combined sources7
Beta strandi80 – 86Combined sources7
Beta strandi88 – 91Combined sources4
Beta strandi93 – 100Combined sources8
Beta strandi102 – 106Combined sources5
Turni110 – 112Combined sources3
Beta strandi120 – 123Combined sources4
Beta strandi125 – 127Combined sources3
Beta strandi129 – 132Combined sources4
Beta strandi134 – 137Combined sources4
Beta strandi145 – 148Combined sources4
Beta strandi161 – 164Combined sources4
Beta strandi166 – 168Combined sources3
Beta strandi172 – 174Combined sources3
Beta strandi176 – 179Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi204 – 207Combined sources4
Beta strandi211 – 213Combined sources3
Beta strandi217 – 220Combined sources4
Beta strandi231 – 234Combined sources4
Beta strandi236 – 240Combined sources5
Beta strandi242 – 253Combined sources12
Beta strandi255 – 258Combined sources4
Beta strandi260 – 263Combined sources4
Beta strandi265 – 272Combined sources8
Beta strandi277 – 280Combined sources4
Beta strandi282 – 285Combined sources4
Beta strandi287 – 290Combined sources4
Beta strandi295 – 297Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi303 – 306Combined sources4
Beta strandi308 – 314Combined sources7
Turni316 – 319Combined sources4
Beta strandi320 – 325Combined sources6
Beta strandi338 – 344Combined sources7
Beta strandi346 – 349Combined sources4
Beta strandi351 – 358Combined sources8
Helixi361 – 370Combined sources10
Beta strandi380 – 385Combined sources6
Beta strandi387 – 389Combined sources3
Beta strandi398 – 400Combined sources3
Beta strandi408 – 413Combined sources6
Beta strandi415 – 419Combined sources5
Beta strandi422 – 424Combined sources3
Helixi431 – 433Combined sources3
Helixi452 – 458Combined sources7
Helixi467 – 469Combined sources3
Helixi482 – 485Combined sources4
Helixi490 – 502Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBGX-ray1.70A1-506[»]
1DBOX-ray1.70A1-506[»]
1OFLX-ray1.70A27-506[»]
1OFMX-ray1.80A27-506[»]
SMRiQ46079.
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)DescriptionActionsGraphical viewLength
Sequence conflicti195A → G in AAC83384 (PubMed:10618199).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DBGX-ray1.70A1-506[»]
1DBOX-ray1.70A1-506[»]
1OFLX-ray1.70A27-506[»]
1OFMX-ray1.80A27-506[»]
SMRiQ46079.
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.
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: November 2, 2016
This is version 93 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.