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Q56F26

- EBDG_AMYOR

UniProt

Q56F26 - EBDG_AMYOR

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Protein

Exo-beta-D-glucosaminidase

Gene

csxA

Organism
Amycolatopsis orientalis (Nocardia orientalis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

pH dependencei

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 8.0.2 Publications

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei469 – 4691Proton donor1 Publication
Active sitei541 – 5411Nucleophile1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. exo-1,4-beta-D-glucosaminidase activity Source: UniProtKB-EC
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: UniProtKB

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-KW
  2. polysaccharide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.165. 315.

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Exo-beta-D-glucosaminidaseImported (EC:3.2.1.165)
Short name:
GlcNase1 Publication
Alternative name(s):
Exochitinase1 Publication
Gene namesi
Name:csxAImported
OrganismiAmycolatopsis orientalis (Nocardia orientalis)
Taxonomic identifieri31958 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

Subcellular locationi

Secretedextracellular space 2 Publications

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Propeptidei33 – 46141 PublicationSequence AnalysisPRO_0000399046Add
BLAST
Chaini47 – 1032986Exo-beta-D-glucosaminidase1 PublicationPRO_5000095799Add
BLAST

Interactioni

Subunit structurei

Monomer.3 Publications

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533
Beta strandi56 – 616
Helixi62 – 643
Helixi68 – 703
Beta strandi82 – 854
Helixi90 – 967
Helixi108 – 1114
Helixi115 – 1173
Beta strandi121 – 13010
Beta strandi133 – 1408
Beta strandi143 – 1519
Beta strandi154 – 1574
Turni159 – 1613
Beta strandi162 – 1643
Beta strandi169 – 1724
Turni174 – 1763
Beta strandi179 – 18810
Turni193 – 1953
Beta strandi196 – 1983
Turni202 – 2043
Turni209 – 2124
Beta strandi219 – 23820
Beta strandi242 – 25514
Beta strandi257 – 2593
Beta strandi261 – 2699
Beta strandi272 – 2809
Beta strandi285 – 2895
Beta strandi293 – 2975
Turni304 – 3063
Beta strandi312 – 3209
Beta strandi323 – 33210
Beta strandi337 – 3415
Beta strandi347 – 3515
Beta strandi354 – 3563
Beta strandi358 – 3625
Helixi373 – 38513
Beta strandi390 – 3956
Helixi400 – 40910
Beta strandi412 – 4165
Beta strandi419 – 4213
Helixi422 – 4243
Turni425 – 4273
Beta strandi431 – 4333
Helixi440 – 45516
Beta strandi464 – 4663
Beta strandi468 – 4703
Helixi474 – 48613
Beta strandi493 – 4953
Beta strandi497 – 4993
Beta strandi503 – 5053
Helixi521 – 5255
Beta strandi534 – 5429
Helixi551 – 5577
Helixi560 – 5689
Turni575 – 5773
Beta strandi579 – 5813
Helixi587 – 59711
Helixi603 – 62826
Beta strandi632 – 6343
Beta strandi636 – 6427
Beta strandi647 – 6493
Beta strandi651 – 6533
Helixi664 – 6729
Beta strandi675 – 6806
Turni682 – 6843
Beta strandi686 – 6916
Beta strandi693 – 6953
Beta strandi697 – 70812
Beta strandi713 – 72412
Turni726 – 7283
Beta strandi729 – 7357
Beta strandi744 – 75310
Beta strandi759 – 77012
Helixi776 – 7783
Beta strandi786 – 7883
Helixi793 – 7975
Beta strandi803 – 8119
Beta strandi815 – 82511
Beta strandi828 – 8303
Beta strandi833 – 8419
Beta strandi852 – 8554
Beta strandi857 – 8604
Beta strandi865 – 8739
Helixi874 – 8774
Beta strandi883 – 8886
Turni889 – 8913
Beta strandi892 – 8976
Beta strandi909 – 9124
Helixi913 – 9153
Beta strandi916 – 9249
Beta strandi935 – 9384
Beta strandi945 – 96521
Beta strandi968 – 9703
Beta strandi974 – 9785
Beta strandi981 – 9877
Beta strandi999 – 10079
Beta strandi1009 – 101810
Beta strandi1026 – 10327

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ56F26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56F26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini909 – 1032124CBM6PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Sequence Analysis
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR005084. 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]
PANTHERiPTHR10066:SF9. PTHR10066:SF9. 1 hit.
PfamiPF03422. CBM_6. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q56F26-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSFRQKRTRI PLLAMTVTAL AAAVCGVTTA PAATGAEVAV PLSVGAAAGN
60 70 80 90 100
ATPIPGYVIQ SSAQVSDDSA VSKPGFPTSG WYPVSSRSTV YAGLLQNGKY
110 120 130 140 150
ADPFYSTNMQ NVPAAQFSVP WWYRTDLNVD DTSSRTYLDF SGVLSKADVW
160 170 180 190 200
VNGTKVATKD QVNGAYTRHD LDITAQVHTG VNSVAFKVYP NDPNRDLSMG
210 220 230 240 250
WIDWAQTPPD QNMGIVRDVL VRRSGAVALR SAHVIQKLNS ALDHADLTVK
260 270 280 290 300
ADVRNDSANA VQTTVAGTVA GKPISQTVSL AAKERKTVTF PLVGLDRPNV
310 320 330 340 350
WWPAGMGGQH RYDLDLTASV GGTPSDAAKS KFGVRDVKAT LNSSGGRQYS
360 370 380 390 400
VNGKPLLIRG GGYTPDLFLR WNETAAADKL KYVLNLGLNT VRLEGHIEPD
410 420 430 440 450
EFFDIADDLG VLTMPGWECC DKWEGQVNGE EKGEPWVESD YPIAKASMFS
460 470 480 490 500
EAERLRDHPS VISFHIGSDF APDRRIEQGY LDAMKAADFL LPVIPAASAR
510 520 530 540 550
PSPITGASGM KMNGPYDYVP PVYWYDKSQK DRGGAWSFNS ETSAGVDIPT
560 570 580 590 600
MDTLKRMMSA SELDTMWKNP SAKQYHRSSS DTFGNLKLFG DALTKRYGAS
610 620 630 640 650
ANLNDFVRKA QLSQYENVRA EFESHSRNYT DSTNPSTGLI YWMLNSPWTS
660 670 680 690 700
LHWQLFDAYM DQNGAYYGAK KANEPLHIQY SHDNRSVVVI NQTSNAVSGL
710 720 730 740 750
TATTKLYNLD GTEKYSNTKT GLSVGALGAK ATAVTVPAVS GLSTTYLAKW
760 770 780 790 800
VLTDSSGKEV SRNVYWLSTK ADTLNWGGSD WYYTPQSAFA DLSGLNNLGQ
810 820 830 840 850
SAVGATANSV AGADGTTTTT VTLKNTSGGR LPAFYVDSKV VDSAGKPVLP
860 870 880 890 900
VEWNDNAVSL WPGETTTLTA KYRTADLKGS KPSVRISGWN TGTQTVPADG
910 920 930 940 950
SGPGPSDPVD YQAEDATIVQ GAVESNHAGY TGTGFVNYDN VAGSSVEWTV
960 970 980 990 1000
TVPSAGTYDV VVRYANGTTT SRPLDFSVNG SISASGVAFG STGTWPAWTT
1010 1020 1030
KTVRVTLAAG VNKIKAVATT ANGGPNVDKI TL
Length:1,032
Mass (Da):110,633
Last modified:March 21, 2006 - v2
Checksum:i150778589094F223
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581V → VN AA sequence (PubMed:16316314)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY962188 Genomic DNA. Translation: AAX62629.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY962188 Genomic DNA. Translation: AAX62629.2 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q56F26.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.165. 315.

Miscellaneous databases

EvolutionaryTracei Q56F26.

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR005084. 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 ]
PANTHERi PTHR10066:SF9. PTHR10066:SF9. 1 hit.
Pfami PF03422. CBM_6. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51175. CBM6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiEBDG_AMYOR
AccessioniPrimary (citable) accession number: Q56F26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 21, 2006
Last modified: October 29, 2014
This is version 57 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, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3