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Q56F26

- EBDG_AMYOR

UniProt

Q56F26 - EBDG_AMYOR

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
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      Previous versions | rss
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    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

    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
    2. extracellular space Source: UniProtKB-SubCell

    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

    MSFRQKRTRI PLLAMTVTAL AAAVCGVTTA PAATGAEVAV PLSVGAAAGN     50
    ATPIPGYVIQ SSAQVSDDSA VSKPGFPTSG WYPVSSRSTV YAGLLQNGKY 100
    ADPFYSTNMQ NVPAAQFSVP WWYRTDLNVD DTSSRTYLDF SGVLSKADVW 150
    VNGTKVATKD QVNGAYTRHD LDITAQVHTG VNSVAFKVYP NDPNRDLSMG 200
    WIDWAQTPPD QNMGIVRDVL VRRSGAVALR SAHVIQKLNS ALDHADLTVK 250
    ADVRNDSANA VQTTVAGTVA GKPISQTVSL AAKERKTVTF PLVGLDRPNV 300
    WWPAGMGGQH RYDLDLTASV GGTPSDAAKS KFGVRDVKAT LNSSGGRQYS 350
    VNGKPLLIRG GGYTPDLFLR WNETAAADKL KYVLNLGLNT VRLEGHIEPD 400
    EFFDIADDLG VLTMPGWECC DKWEGQVNGE EKGEPWVESD YPIAKASMFS 450
    EAERLRDHPS VISFHIGSDF APDRRIEQGY LDAMKAADFL LPVIPAASAR 500
    PSPITGASGM KMNGPYDYVP PVYWYDKSQK DRGGAWSFNS ETSAGVDIPT 550
    MDTLKRMMSA SELDTMWKNP SAKQYHRSSS DTFGNLKLFG DALTKRYGAS 600
    ANLNDFVRKA QLSQYENVRA EFESHSRNYT DSTNPSTGLI YWMLNSPWTS 650
    LHWQLFDAYM DQNGAYYGAK KANEPLHIQY SHDNRSVVVI NQTSNAVSGL 700
    TATTKLYNLD GTEKYSNTKT GLSVGALGAK ATAVTVPAVS GLSTTYLAKW 750
    VLTDSSGKEV SRNVYWLSTK ADTLNWGGSD WYYTPQSAFA DLSGLNNLGQ 800
    SAVGATANSV AGADGTTTTT VTLKNTSGGR LPAFYVDSKV VDSAGKPVLP 850
    VEWNDNAVSL WPGETTTLTA KYRTADLKGS KPSVRISGWN TGTQTVPADG 900
    SGPGPSDPVD YQAEDATIVQ GAVESNHAGY TGTGFVNYDN VAGSSVEWTV 950
    TVPSAGTYDV VVRYANGTTT SRPLDFSVNG SISASGVAFG STGTWPAWTT 1000
    KTVRVTLAAG VNKIKAVATT ANGGPNVDKI TL 1032
    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 1, 2014
    This is version 56 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