Exo-beta-D-glucosaminidase precursor - Amycolatopsis orientalis

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Q56F26 (EBDG_AMYOR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Exo-beta-D-glucosaminidase
Short name=GlcNase
EC=3.2.1.165

Alternative name(s):
Exochitinase

Gene names

Name:

csxA

Organism

Amycolatopsis orientalis (Nocardia orientalis)

Taxonomic identifier

31958 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis

Protein attributes

Sequence length	1032 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular 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

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro exo-1,4-beta-D-glucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

Potential

Propeptide

33 – 46

Ref.1

PRO_0000399046

Chain

47 – 1032

986

Exo-beta-D-glucosaminidase Ref.1

PRO_5000095799

Regions

Domain

909 – 1032

124

CBM6

Sites

Active site

469

Proton donor Ref.3

Active site

541

Nucleophile Ref.3

Experimental info

Sequence conflict

V → VN AA sequence Ref.1

Secondary structure

1032

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q56F26 [UniParc].

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

FASTA

1,032

110,633

        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: 16316314] [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: 2351651] [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: 18976664] [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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VZO	X-ray	2.24	A/B	2-1032	[»]
2VZP	X-ray	1.05	A/B	906-1032	[»]
2VZQ	X-ray	1.70	A/B	906-1032	[»]
2VZR	X-ray	1.95	A/B	906-1032	[»]
2VZS	X-ray	1.85	A/B	2-1032	[»]
2VZT	X-ray	2.20	A/B	2-1032	[»]
2VZU	X-ray	2.10	A/B	2-1032	[»]
2VZV	X-ray	2.70	A/B	2-1032	[»]
2X05	X-ray	2.30	A/B	2-1032	[»]
2X09	X-ray	2.40	A/B	2-1032	[»]

ProteinModelPortal

Q56F26.

ModBase

Search...

Protein family/group databases

CAZy

CBM35. Carbohydrate-Binding Module Family 35.
GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.165. 315.

Family and domain databases

InterPro

IPR005084. CMB_fam6.
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_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

Pfam

PF03422. CBM_6. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 2 hits.
SSF49303. Glyco_hydro_2Ig. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51175. CBM6. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

EBDG_AMYOR

Accession

Primary (citable) accession number: Q56F26

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	March 21, 2006
Last modified:	December 14, 2011
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents