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Q56F26 (EBDG_AMYOR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exo-beta-D-glucosaminidase

Short name=GlcNase
EC=3.2.1.165
Alternative name(s):
Exochitinase
Gene names
Name:csxA
OrganismAmycolatopsis orientalis (Nocardia orientalis)
Taxonomic identifier31958 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

Protein attributes

Sequence length1032 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide. Ref.1 Ref.2

Catalytic activity

Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini. Ref.1 Ref.2

Subunit structure

Monomer. Ref.1 Ref.2

Subcellular location

Secretedextracellular space Ref.1 Ref.2.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family.

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5 with chitotriitol as substrate, and 5.3 with (GlcN)2 as substrate. Activity is lost below pH 3.5 and above pH 8.0. Ref.1 Ref.2

Temperature dependence:

Optimum temperature is 60 degrees Celsius. Stable below 50 degrees Celsius, inactive above 60 degrees Celsius. Ref.1 Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Propeptide33 – 4614 Ref.1
PRO_0000399046
Chain47 – 1032986Exo-beta-D-glucosaminidase Ref.1
PRO_5000095799

Regions

Domain909 – 1032124CBM6

Sites

Active site4691Proton donor Ref.3
Active site5411Nucleophile Ref.3

Experimental info

Sequence conflict581V → VN AA sequence Ref.1

Secondary structure

......................................................................................................................................................................................... 1032
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56F26 [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: 150778589094F223

FASTA1,032110,633
        10         20         30         40         50         60 
MSFRQKRTRI PLLAMTVTAL AAAVCGVTTA PAATGAEVAV PLSVGAAAGN ATPIPGYVIQ 

        70         80         90        100        110        120 
SSAQVSDDSA VSKPGFPTSG WYPVSSRSTV YAGLLQNGKY ADPFYSTNMQ NVPAAQFSVP 

       130        140        150        160        170        180 
WWYRTDLNVD DTSSRTYLDF SGVLSKADVW VNGTKVATKD QVNGAYTRHD LDITAQVHTG 

       190        200        210        220        230        240 
VNSVAFKVYP NDPNRDLSMG WIDWAQTPPD QNMGIVRDVL VRRSGAVALR SAHVIQKLNS 

       250        260        270        280        290        300 
ALDHADLTVK ADVRNDSANA VQTTVAGTVA GKPISQTVSL AAKERKTVTF PLVGLDRPNV 

       310        320        330        340        350        360 
WWPAGMGGQH RYDLDLTASV GGTPSDAAKS KFGVRDVKAT LNSSGGRQYS VNGKPLLIRG 

       370        380        390        400        410        420 
GGYTPDLFLR WNETAAADKL KYVLNLGLNT VRLEGHIEPD EFFDIADDLG VLTMPGWECC 

       430        440        450        460        470        480 
DKWEGQVNGE EKGEPWVESD YPIAKASMFS EAERLRDHPS VISFHIGSDF APDRRIEQGY 

       490        500        510        520        530        540 
LDAMKAADFL LPVIPAASAR PSPITGASGM KMNGPYDYVP PVYWYDKSQK DRGGAWSFNS 

       550        560        570        580        590        600 
ETSAGVDIPT MDTLKRMMSA SELDTMWKNP SAKQYHRSSS DTFGNLKLFG DALTKRYGAS 

       610        620        630        640        650        660 
ANLNDFVRKA QLSQYENVRA EFESHSRNYT DSTNPSTGLI YWMLNSPWTS LHWQLFDAYM 

       670        680        690        700        710        720 
DQNGAYYGAK KANEPLHIQY SHDNRSVVVI NQTSNAVSGL TATTKLYNLD GTEKYSNTKT 

       730        740        750        760        770        780 
GLSVGALGAK ATAVTVPAVS GLSTTYLAKW VLTDSSGKEV SRNVYWLSTK ADTLNWGGSD 

       790        800        810        820        830        840 
WYYTPQSAFA DLSGLNNLGQ SAVGATANSV AGADGTTTTT VTLKNTSGGR LPAFYVDSKV 

       850        860        870        880        890        900 
VDSAGKPVLP VEWNDNAVSL WPGETTTLTA KYRTADLKGS KPSVRISGWN TGTQTVPADG 

       910        920        930        940        950        960 
SGPGPSDPVD YQAEDATIVQ GAVESNHAGY TGTGFVNYDN VAGSSVEWTV TVPSAGTYDV 

       970        980        990       1000       1010       1020 
VVRYANGTTT SRPLDFSVNG SISASGVAFG STGTWPAWTT KTVRVTLAAG VNKIKAVATT 

      1030 
ANGGPNVDKI TL 

« Hide

References

[1]"Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases."
Cote N., Fleury A., Dumont-Blanchette E., Fukamizo T., Mitsutomi M., Brzezinski R.
Biochem. J. 394:675-686(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 47-60 AND 610-619, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
Strain: ATCC 19795 / DSM 40040 / JCM 4235 / NBRC 12806.
[2]"Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis."
Nanjo F., Katsumi R., Sakai K.
J. Biol. Chem. 265:10088-10094(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION.
[3]"The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis."
van Bueren A.L., Ghinet M.G., Gregg K., Fleury A., Brzezinski R., Boraston A.B.
J. Mol. Biol. 385:131-139(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-1032 IN COMPLEX WITH BETA-1,4-D-GLUCOSAMINE TETRASACCHARIDE, ACTIVE SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY962188 Genomic DNA. Translation: AAX62629.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VZOX-ray2.24A/B2-1032[»]
2VZPX-ray1.05A/B906-1032[»]
2VZQX-ray1.70A/B906-1032[»]
2VZRX-ray1.95A/B906-1032[»]
2VZSX-ray1.85A/B2-1032[»]
2VZTX-ray2.20A/B2-1032[»]
2VZUX-ray2.10A/B2-1032[»]
2VZVX-ray2.70A/B2-1032[»]
2X05X-ray2.30A/B2-1032[»]
2X09X-ray2.40A/B2-1032[»]
ProteinModelPortalQ56F26.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM35. Carbohydrate-Binding Module Family 35.
GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.165. 315.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR005084. CMB_fam6.
IPR028829. Exo-b-D-glucosamin.
IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10066:SF9. PTHR10066:SF9. 1 hit.
PfamPF03422. CBM_6. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ56F26.

Entry information

Entry nameEBDG_AMYOR
AccessionPrimary (citable) accession number: Q56F26
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 21, 2006
Last modified: March 19, 2014
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries