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Q12624

- GUN3_HUMIN

UniProt

Q12624 - GUN3_HUMIN

Protein

Endoglucanase 3

Gene

CMC3

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 sitei215 – 2151Proton donorBy similarity
    Active sitei322 – 3221NucleophileBy 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

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH5. Glycoside Hydrolase Family 5.
    mycoCLAPiEGL5C_HUMGT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase 3 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase 3
    Endo-1,4-beta-glucanase 3
    Gene namesi
    Name:CMC3
    OrganismiHumicola insolens (Soft-rot fungus)
    Taxonomic identifieri34413 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    Pathology & Biotechi

    Biotechnological usei

    Used as a detergent cellulase. Sold under the name Celluzyme by Novozymes. This special enzyme has three effects: colour brightening, softening and removal of particulate soil. The overall effect is that it helps to preserve the nice appearance of new fabric and restores old fabric so that it looks new again.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 388372Endoglucanase 3PRO_0000007863Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 41By similarity
    Disulfide bondi35 ↔ 51By similarity
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ12624.
    SMRiQ12624. Positions 19-52, 86-387.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 5236CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 9139LinkerAdd
    BLAST
    Regioni92 – 388297CatalyticAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000254. Cellulose-bd_dom_fun.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view]
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q12624-1 [UniParc]FASTAAdd to Basket

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    MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ    50
    CQPQPTTLRT TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK 100
    GEYPGLWGKH FTFPSTSSIQ THINDGFNMF RVAFSMERLA PNQLNAAFDA 150
    NYLRNLTETV NFITGKGKYA MLDPHNFGRY YERIITDKAA FASFFTKLAT 200
    HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA TSQYIMVEGN 250
    SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG 300
    LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT 350
    GALWWAGGPW WGDYIYSFEP PSGIGYTYYN SLLKKYVP 388
    Length:388
    Mass (Da):42,564
    Last modified:November 1, 1996 - v1
    Checksum:iC7CF349DACC10690
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81G → S in BAA12676. (PubMed:9058960)Curated
    Sequence conflicti340 – 3401T → N in BAA12676. (PubMed:9058960)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76046 Genomic DNA. Translation: CAA53631.1.
    D84470 Genomic DNA. Translation: BAA12676.1.
    PIRiJC5461.
    S43920.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76046 Genomic DNA. Translation: CAA53631.1 .
    D84470 Genomic DNA. Translation: BAA12676.1 .
    PIRi JC5461.
    S43920.

    3D structure databases

    ProteinModelPortali Q12624.
    SMRi Q12624. Positions 19-52, 86-387.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH5. Glycoside Hydrolase Family 5.
    mycoCLAPi EGL5C_HUMGT.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR001547. Glyco_hydro_5.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF00150. Cellulase. 1 hit.
    [Graphical view ]
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel method for efficient expression cloning of fungal enzyme genes."
      Dalboege H., Hansen H.P.H.
      Mol. Gen. Genet. 243:253-260(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning, sequencing, and expression of a thermostable cellulase gene of Humicola grisea."
      Takashima S., Nakamura A., Masaki H., Uozumi T.
      Biosci. Biotechnol. Biochem. 61:245-250(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: IFO 9854.

    Entry informationi

    Entry nameiGUN3_HUMIN
    AccessioniPrimary (citable) accession number: Q12624
    Secondary accession number(s): Q12620
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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