Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9C1S9

- GUX6_HUMIN

UniProt

Q9C1S9 - GUX6_HUMIN

Protein

Exoglucanase-6A

Gene

cel6A

Organism
Humicola insolens (Soft-rot fungus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a central role in the recycling of plant biomass. 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.1 Publication

    Catalytic activityi

    Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei163 – 1631Substrate3 Publications
    Binding sitei165 – 1651Substrate3 Publications
    Active sitei252 – 2521Proton donor2 PublicationsPROSITE-ProRule annotation
    Binding sitei297 – 2971Substrate3 Publications
    Binding sitei300 – 3001Substrate3 Publications
    Binding sitei336 – 3361Substrate3 Publications
    Binding sitei397 – 3971Substrate3 Publications
    Binding sitei425 – 4251Substrate3 Publications
    Binding sitei429 – 4291Substrate3 Publications
    Active sitei431 – 4311Proton acceptor3 PublicationsPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase 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.
    GH6. Glycoside Hydrolase Family 6.
    mycoCLAPiCBH6A_HUMIN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase-6A (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase 6A
    Avicelase 2
    Beta-glucancellobiohydrolase 6A
    Exocellobiohydrolase 6A
    Gene namesi
    Name:cel6A4 Publications
    Synonyms:avi2Imported
    OrganismiHumicola insolens (Soft-rot fungus)
    Taxonomic identifieri34413 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 476460Exoglucanase-6APRO_0000248843Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 50Sequence Analysis
    Disulfide bondi44 ↔ 60Sequence Analysis
    Glycosylationi144 – 1441O-linked (Man...)1 Publication
    Glycosylationi153 – 1531O-linked (Man...)1 Publication
    Glycosylationi167 – 1671N-linked (GlcNAc...)4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.4 Publications

    Structurei

    Secondary structure

    1
    476
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni119 – 1224
    Beta strandi123 – 1253
    Helixi129 – 1379
    Helixi140 – 1423
    Helixi146 – 15510
    Beta strandi162 – 1643
    Helixi167 – 1693
    Turni170 – 1723
    Helixi173 – 18614
    Beta strandi193 – 1997
    Beta strandi209 – 2113
    Helixi218 – 2203
    Helixi222 – 23918
    Turni240 – 2423
    Beta strandi245 – 2495
    Helixi255 – 2595
    Helixi264 – 28320
    Beta strandi289 – 2946
    Turni298 – 3025
    Helixi304 – 32017
    Beta strandi327 – 3337
    Helixi347 – 3493
    Helixi357 – 37014
    Beta strandi376 – 3805
    Beta strandi385 – 3884
    Beta strandi398 – 4025
    Beta strandi418 – 4225
    Helixi443 – 4464
    Helixi462 – 4709

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BVWX-ray1.92A117-476[»]
    1GZ1X-ray1.90A115-476[»]
    1OC5X-ray1.70A113-476[»]
    1OC6X-ray1.50A113-476[»]
    1OC7X-ray1.11A113-476[»]
    1OCBX-ray1.75A/B115-476[»]
    1OCJX-ray1.30A115-476[»]
    1OCNX-ray1.31A115-476[»]
    2BVWX-ray1.70A/B115-476[»]
    4I5RX-ray1.50A117-157[»]
    4I5UX-ray1.22A117-161[»]
    ProteinModelPortaliQ9C1S9.
    SMRiQ9C1S9. Positions 30-61, 116-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9C1S9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 6028CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 22223Substrate binding loop 13 PublicationsAdd
    BLAST
    Regioni423 – 46139Substrate binding loop 23 PublicationsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi73 – 786Poly-SerSequence Analysis

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 6 (cellulase A) family.Sequence Analysis
    Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.20.20.40. 1 hit.
    InterProiIPR016288. Beta_cellobiohydrolase.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001524. Glyco_hydro_6_CS.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF01341. Glyco_hydro_6. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
    PRINTSiPR00733. GLHYDRLASE6.
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51989. SSF51989. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEiPS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
    PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9C1S9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKFFLTAAF AAAALAAPVV EERQNCAPTW GQCGGIGFNG PTCCQSGSTC    50
    VKQNDWYSQC LPGSQVTTTS TTSTSSSSTT SRATSTTRTG GVTSITTAPT 100
    RTVTIPGGAT TTASYNGNPF EGVQLWANNY YRSEVHTLAI PQITDPALRA 150
    AASAVAEVPS FQWLDRNVTV DTLLVETLSE IRAANQAGAN PPYAAQIVVY 200
    DLPDRDCAAA ASNGEWAIAN NGANNYKGYI NRIREILISF SDVRTILVIE 250
    PDSLANMVTN MNVAKCSGAA STYRELTIYA LKQLDLPHVA MYMDAGHAGW 300
    LGWPANIQPA AELFAKIYED AGKPRAVRGL ATNVANYNAW SISSPPPYTS 350
    PNPNYDEKHY IEAFRPLLEA RGFPAQFIVD QGRSGKQPTG QKEWGHWCNA 400
    IGTGFGMRPT ANTGHQYVDA FVWVKPGGEC DGTSDTTAAR YDYHCGLEDA 450
    LKPAPEAGQW FQAYFEQLLR NANPPF 476
    Length:476
    Mass (Da):51,276
    Last modified:June 1, 2001 - v1
    Checksum:iD2B0054F1381E653
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048710 Genomic DNA. Translation: BAB39154.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB048710 Genomic DNA. Translation: BAB39154.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BVW X-ray 1.92 A 117-476 [» ]
    1GZ1 X-ray 1.90 A 115-476 [» ]
    1OC5 X-ray 1.70 A 113-476 [» ]
    1OC6 X-ray 1.50 A 113-476 [» ]
    1OC7 X-ray 1.11 A 113-476 [» ]
    1OCB X-ray 1.75 A/B 115-476 [» ]
    1OCJ X-ray 1.30 A 115-476 [» ]
    1OCN X-ray 1.31 A 115-476 [» ]
    2BVW X-ray 1.70 A/B 115-476 [» ]
    4I5R X-ray 1.50 A 117-157 [» ]
    4I5U X-ray 1.22 A 117-161 [» ]
    ProteinModelPortali Q9C1S9.
    SMRi Q9C1S9. Positions 30-61, 116-476.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH6. Glycoside Hydrolase Family 6.
    mycoCLAPi CBH6A_HUMIN.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9C1S9.

    Family and domain databases

    Gene3Di 3.20.20.40. 1 hit.
    InterProi IPR016288. Beta_cellobiohydrolase.
    IPR000254. Cellulose-bd_dom_fun.
    IPR001524. Glyco_hydro_6_CS.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF01341. Glyco_hydro_6. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
    PRINTSi PR00733. GLHYDRLASE6.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51989. SSF51989. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
    PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and overexpression of the avi2 gene encoding a major cellulase produced by Humicola insolens FERM BP-5977."
      Moriya T., Watanabe M., Sumida N., Okakura K., Murakami T.
      Biosci. Biotechnol. Biochem. 67:1434-1437(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FERM BP-5977.
    2. "Enzymatic properties of cellulases from Humicola insolens."
      Schuelein M.
      J. Biotechnol. 57:71-81(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    3. "Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding."
      Varrot A., Schuelein M., Davies G.J.
      Biochemistry 38:8884-8891(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 115-476 IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-167.
    4. "Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A."
      Varrot A., Frandsen T.P., Driguez H., Davies G.J.
      Acta Crystallogr. D 58:2201-2204(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-476 OF MUTANT ALA-416 IN COMPLEX WITH SUBSTRATE ANALOG, GLYCOSYLATION AT ASN-167.
    5. "Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens."
      Varrot A., Frandsen T.P., von Ossowski I., Boyer V., Cottaz S., Driguez H., Schuelein M., Davies G.J.
      Structure 11:855-864(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 113-476 OF MUTANT ASN-431 IN COMPLEX WITH SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-167.
    6. "Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution."
      Varrot A., Hastrup S., Schuelein M., Davies G.J.
      Biochem. J. 337:297-304(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-476, FUNCTION, SUBUNIT, GLYCOSYLATION AT THR-144; SER-153 AND ASN-167.

    Entry informationi

    Entry nameiGUX6_HUMIN
    AccessioniPrimary (citable) accession number: Q9C1S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 59 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