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P56680

- GUN1_HUMIN

UniProt

P56680 - GUN1_HUMIN

Protein

Endoglucanase 1

Gene

CEL7B

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (15 Jul 1999)
      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 sitei197 – 1971Nucleophile
    Active sitei202 – 2021Proton donor

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17623.

    Protein family/group databases

    CAZyiGH7. Glycoside Hydrolase Family 7.
    mycoCLAPiEGL7B_HUMIN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endoglucanase 1 (EC:3.2.1.4)
    Alternative name(s):
    Cellulase 1
    Endo-1,4-beta-glucanase 1
    Endoglucanase I
    Gene namesi
    Name:CEL7B
    OrganismiHumicola insolens (Soft-rot fungus)
    Taxonomic identifieri34413 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Protein family/group databases

    Allergomei8280. Hum in Cellulase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 402402Endoglucanase 1PRO_0000184057Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Pyrrolidone carboxylic acid
    Disulfide bondi18 ↔ 24
    Disulfide bondi51 ↔ 73
    Disulfide bondi63 ↔ 69
    Glycosylationi89 – 891N-linked (GlcNAc...)
    Disulfide bondi140 ↔ 365
    Disulfide bondi172 ↔ 195
    Disulfide bondi176 ↔ 194
    Disulfide bondi215 ↔ 234
    Disulfide bondi223 ↔ 228
    Disulfide bondi239 ↔ 315
    Glycosylationi247 – 2471N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 198
    Turni20 – 223
    Beta strandi23 – 3311
    Helixi35 – 373
    Beta strandi40 – 423
    Turni60 – 623
    Helixi66 – 727
    Beta strandi73 – 753
    Helixi81 – 844
    Beta strandi86 – 894
    Beta strandi92 – 987
    Beta strandi108 – 1125
    Beta strandi116 – 1194
    Beta strandi127 – 1348
    Beta strandi143 – 1497
    Turni153 – 1564
    Helixi164 – 1674
    Beta strandi180 – 1823
    Beta strandi192 – 1943
    Beta strandi197 – 2037
    Beta strandi208 – 2136
    Beta strandi215 – 2195
    Beta strandi221 – 2233
    Helixi225 – 2284
    Beta strandi232 – 2343
    Helixi243 – 2464
    Beta strandi250 – 2556
    Beta strandi258 – 2614
    Beta strandi266 – 2749
    Beta strandi280 – 28910
    Beta strandi292 – 2943
    Beta strandi308 – 3103
    Helixi312 – 3176
    Helixi321 – 3255
    Helixi328 – 33811
    Beta strandi340 – 3478
    Turni350 – 3545
    Helixi355 – 3584
    Helixi360 – 3623
    Turni367 – 3704
    Helixi372 – 3787
    Beta strandi383 – 39311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A39X-ray2.20A2-402[»]
    1DYMX-ray1.75A2-402[»]
    1OJIX-ray2.15A2-402[»]
    1OJJX-ray1.40A/B2-402[»]
    1OJKX-ray1.50A/B2-402[»]
    2A39X-ray2.20A/B2-398[»]
    ProteinModelPortaliP56680.
    SMRiP56680. Positions 1-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56680.

    Family & Domainsi

    Sequence similaritiesi

    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.

    P56680-1 [UniParc]FASTAAdd to Basket

    « Hide

    QKPGETKEVH PQLTTFRCTK RGGCKPATNF IVLDSLSHPI HRAEGLGPGG    50
    CGDWGNPPPK DVCPDVESCA KNCIMEGIPD YSQYGVTTNG TSLRLQHILP 100
    DGRVPSPRVY LLDKTKRRYE MLHLTGFEFT FDVDATKLPC GMNSALYLSE 150
    MHPTGAKSKY NPGGAYYGTG YCDAQCFVTP FINGLGNIEG KGSCCNEMDI 200
    WEANSRASHV APHTCNKKGL YLCEGEECAF EGVCDKNGCG WNNYRVNVTD 250
    YYGRGEEFKV NTLKPFTVVT QFLANRRGKL EKIHRFYVQD GKVIESFYTN 300
    KEGVPYTNMI DDEFCEATGS RKYMELGATQ GMGEALTRGM VLAMSIWWDQ 350
    GGNMEWLDHG EAGPCAKGEG APSNIVQVEP FPEVTYTNLR WGEIGSTYQE 400
    LQ 402
    Length:402
    Mass (Da):44,577
    Last modified:July 15, 1999 - v1
    Checksum:iE0C6D31375D1635F
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A39 X-ray 2.20 A 2-402 [» ]
    1DYM X-ray 1.75 A 2-402 [» ]
    1OJI X-ray 2.15 A 2-402 [» ]
    1OJJ X-ray 1.40 A/B 2-402 [» ]
    1OJK X-ray 1.50 A/B 2-402 [» ]
    2A39 X-ray 2.20 A/B 2-398 [» ]
    ProteinModelPortali P56680.
    SMRi P56680. Positions 1-398.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 8280. Hum in Cellulase.
    CAZyi GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi EGL7B_HUMIN.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17623.

    Miscellaneous databases

    EvolutionaryTracei P56680.

    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. "Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites."
      Davies G.J., Ducros V., Lewis R.J., Borchert T.V., Schuelein M.
      J. Biotechnol. 57:91-100(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT TRP-37/TRP-39.
    2. "Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2 A resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate."
      MacKenzie L.F., Sulzenbacher G., Divne C., Jones T.A., Woeldike H.F., Schuelein M., Withers S.G., Davies G.J.
      Biochem. J. 335:409-416(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), MUTAGENESIS.

    Entry informationi

    Entry nameiGUN1_HUMIN
    AccessioniPrimary (citable) accession number: P56680
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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