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P28622

- GUN4_BACS5

UniProt

P28622 - GUN4_BACS5

Protein

Endoglucanase 4

Gene
N/A
Organism
Bacillus sp. (strain KSM-522)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei400 – 4001By similarity
    Active sitei438 – 4381By similarity
    Active sitei447 – 4471By similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Protein family/group databases

    CAZyiCBM3. Carbohydrate-Binding Module Family 3.
    GH9. Glycoside Hydrolase Family 9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase 4 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase 4
    EG-IV
    Endo-1,4-beta-glucanase 4
    OrganismiBacillus sp. (strain KSM-522)
    Taxonomic identifieri120046 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 636611Endoglucanase 4PRO_0000007952Add
    BLAST

    Proteomic databases

    PRIDEiP28622.

    Structurei

    3D structure databases

    ProteinModelPortaliP28622.
    SMRiP28622. Positions 27-634.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini478 – 635158CBM3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM3 (carbohydrate binding type-3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.60.40.710. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    [Graphical view]
    PfamiPF00942. CBM_3. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view]
    SMARTiSM01067. CBM_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF49384. SSF49384. 1 hit.
    PROSITEiPS51172. CBM3. 1 hit.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28622-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP    50
    ESNRLNWRGD SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT 100
    VYEYREAYEE AELLDDMLDQ IKWATDYFLK AHTGPNEFWA QVGDGNADHG 150
    WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT AAALAAGSII FKETDAPYAA 200
    KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE LIWGGIWLYL 250
    ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF 300
    IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA 350
    FVYADWVSDQ EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH 400
    HRTAHGSWSN QLTTPSSHRH TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT 450
    DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE DEFFVEAAVM SNDTTSTQIK 500
    AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV TAVYNEGASL 550
    SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD 600
    ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK 636
    Length:636
    Mass (Da):72,245
    Last modified:May 30, 2000 - v2
    Checksum:i76718BF57A8EF6A2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti530 – 5345AKGFT → CEGIH(PubMed:2113383)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004098 Genomic DNA. Translation: BAA24918.1.
    PIRiJC5874.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004098 Genomic DNA. Translation: BAA24918.1 .
    PIRi JC5874.

    3D structure databases

    ProteinModelPortali P28622.
    SMRi P28622. Positions 27-634.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM3. Carbohydrate-Binding Module Family 3.
    GH9. Glycoside Hydrolase Family 9.

    Proteomic databases

    PRIDEi P28622.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    2.60.40.710. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR008965. Carb-bd_dom.
    IPR001956. CBD_3.
    IPR001701. Glyco_hydro_9.
    IPR018221. Glyco_hydro_9_AS.
    [Graphical view ]
    Pfami PF00942. CBM_3. 1 hit.
    PF00759. Glyco_hydro_9. 1 hit.
    [Graphical view ]
    SMARTi SM01067. CBM_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49384. SSF49384. 1 hit.
    PROSITEi PS51172. CBM3. 1 hit.
    PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
    PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain."
      Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S.
      Biosci. Biotechnol. Biochem. 61:2004-2009(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes."
      Shoseyov O., Foong F., Hamamoto T., Doi R.H.
      Biochem. Biophys. Res. Commun. 169:667-672(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534.
    3. Doi R.H.
      Unpublished observations (JAN-2000)
      Cited for: SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS.

    Entry informationi

    Entry nameiGUN4_BACS5
    AccessioniPrimary (citable) accession number: P28622
    Secondary accession number(s): O50589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 79 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC).1 Publication

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3