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Q12622

- GUN1_HUMGT

UniProt

Q12622 - GUN1_HUMGT

Protein

Endoglucanase EG-1

Gene

EG-1

Organism
Humicola grisea var. thermoidea
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

    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 sitei217 – 2171NucleophileBy similarity
    Active sitei222 – 2221Proton donorBy similarity

    GO - Molecular functioni

    1. cellulase activity Source: UniProtKB-EC

    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

    CAZyiGH7. Glycoside Hydrolase Family 7.
    mycoCLAPiEGL7A_HUMGT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase EG-1 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase
    Endo-1,4-beta-glucanase
    Gene namesi
    Name:EG-1
    OrganismiHumicola grisea var. thermoidea
    Taxonomic identifieri5528 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    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 – 2020By similarityAdd
    BLAST
    Chaini21 – 435415Endoglucanase EG-1PRO_0000007916Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi38 ↔ 44By similarity
    Disulfide bondi71 ↔ 93By similarity
    Disulfide bondi83 ↔ 89By similarity
    Glycosylationi109 – 1091N-linked (GlcNAc...)By similarity
    Disulfide bondi160 ↔ 385By similarity
    Disulfide bondi192 ↔ 215By similarity
    Disulfide bondi196 ↔ 214By similarity
    Disulfide bondi235 ↔ 254By similarity
    Disulfide bondi243 ↔ 248By similarity
    Disulfide bondi259 ↔ 335By similarity
    Glycosylationi267 – 2671N-linked (GlcNAc...)By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Structurei

    3D structure databases

    ProteinModelPortaliQ12622.
    SMRiQ12622. Positions 21-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.70.100.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view]
    PfamiPF00840. Glyco_hydro_7. 1 hit.
    [Graphical view]
    PRINTSiPR00734. GLHYDRLASE7.
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q12622-1 [UniParc]FASTAAdd to Basket

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    MARGTALLGL TSLLLGLVNG QKPGETKEVH PQLTTFRCTK KGGCKPATNY    50
    IVLDSLSHPI HRAEGLGWGN CGDWGNPPPK DVCPDVESCA KNCIMEGIPD 100
    YSQYGVTTNG TSLRLQHILP DGRVPSPRVY LLDKTERRYE MLHLTGFEFT 150
    FDVDATKLPC GMNSALYLSE MHPTGAKSKH NPGGAYYGTG YCDAQCFVTP 200
    FINGLGNIEG KGSCCNEMDI WEANSRASHV APHVCNKKGL YLCEGEECAF 250
    EGVCDKNGCG WNPYRVNVTD YYGRGEEFKV NTLKPFTVVT QFLANRKGKL 300
    EKIHRFYVQD GKIIESFYTN KEGIPYTNMI EDEFCAATGS RKYMELGATQ 350
    GMGEALTRGM VLAMSIWWDQ GGNMEWLDHG EAGPCAKGEG APSNVVQVEP 400
    FPEVTYTNLR WGEIGSTYQE VQKPKPKPGP GPRSD 435
    Length:435
    Mass (Da):47,890
    Last modified:November 1, 1996 - v1
    Checksum:i25EB3D62D96B65FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63516 Genomic DNA. Translation: BAA09786.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63516 Genomic DNA. Translation: BAA09786.1 .

    3D structure databases

    ProteinModelPortali Q12622.
    SMRi Q12622. Positions 21-418.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi EGL7A_HUMGT.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: IFO 9854.

    Entry informationi

    Entry nameiGUN1_HUMGT
    AccessioniPrimary (citable) accession number: Q12622
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 72 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