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P62694

- GUX1_HYPJE

UniProt

P62694 - GUX1_HYPJE

Protein

Exoglucanase 1

Gene

cbh1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei143 – 14311 Publication
    Active sitei229 – 2291Nucleophile1 Publication
    Active sitei234 – 2341Proton donor1 Publication

    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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16499.

    Protein family/group databases

    CAZyiCBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPiCBH7A_TRIRE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase 1 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase I
    Short name:
    CBHI
    Exoglucanase I
    Gene namesi
    Name:cbh1
    OrganismiHypocrea jecorina (Trichoderma reesei)
    Taxonomic identifieri51453 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

    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 – 1717Add
    BLAST
    Chaini18 – 513496Exoglucanase 1PRO_0000007927Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Pyrrolidone carboxylic acid
    Disulfide bondi21 ↔ 89
    Disulfide bondi36 ↔ 42
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi67 ↔ 88
    Disulfide bondi78 ↔ 84
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi155 ↔ 414
    Disulfide bondi189 ↔ 227
    Disulfide bondi193 ↔ 226
    Disulfide bondi247 ↔ 273
    Disulfide bondi255 ↔ 260
    Disulfide bondi278 ↔ 348
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi485 ↔ 502
    Disulfide bondi496 ↔ 512

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 367
    Beta strandi42 – 5110
    Helixi53 – 553
    Beta strandi58 – 603
    Beta strandi66 – 694
    Turni75 – 773
    Helixi81 – 877
    Beta strandi88 – 903
    Helixi95 – 995
    Beta strandi101 – 1044
    Beta strandi107 – 12115
    Beta strandi123 – 1308
    Beta strandi136 – 1383
    Beta strandi142 – 1498
    Beta strandi157 – 1648
    Turni168 – 1747
    Helixi182 – 1843
    Beta strandi198 – 2003
    Beta strandi222 – 2265
    Beta strandi229 – 2357
    Beta strandi240 – 2456
    Beta strandi247 – 2493
    Beta strandi253 – 2564
    Helixi257 – 2604
    Turni262 – 2643
    Beta strandi265 – 2673
    Beta strandi268 – 2736
    Turni282 – 2865
    Beta strandi290 – 2945
    Beta strandi297 – 3004
    Beta strandi305 – 3117
    Beta strandi317 – 3237
    Beta strandi326 – 3294
    Beta strandi333 – 3353
    Beta strandi338 – 3436
    Helixi345 – 35511
    Helixi359 – 3624
    Helixi365 – 37410
    Beta strandi375 – 38511
    Turni387 – 3915
    Helixi392 – 3954
    Beta strandi396 – 3994
    Beta strandi412 – 4143
    Helixi421 – 4277
    Beta strandi432 – 44211
    Turni479 – 4824
    Beta strandi483 – 4897
    Beta strandi498 – 5003
    Beta strandi502 – 5065
    Beta strandi509 – 5124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AZ6NMR-A478-513[»]
    1AZHNMR-A478-513[»]
    1AZJNMR-A478-513[»]
    1AZKNMR-A478-513[»]
    1CBHNMR-A478-513[»]
    1CELX-ray1.80A/B19-451[»]
    1DY4X-ray1.90A19-451[»]
    1EGNX-ray1.60A18-451[»]
    1Q2BX-ray1.60A18-451[»]
    1Q2EX-ray1.75A/B19-451[»]
    2CBHNMR-A478-513[»]
    2CELX-ray2.00A/B19-451[»]
    2V3IX-ray1.05A19-451[»]
    2V3RX-ray1.60A19-451[»]
    3CELX-ray2.00A19-451[»]
    4C4CX-ray1.45A19-451[»]
    4C4DX-ray1.32A19-451[»]
    4CELX-ray2.20A/B19-451[»]
    5CELX-ray1.90A19-451[»]
    6CELX-ray1.70A19-451[»]
    7CELX-ray1.90A19-451[»]
    8CELmodel-A18-451[»]
    ProteinModelPortaliP62694.
    SMRiP62694. Positions 18-451, 478-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62694.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini477 – 51337CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 453436CatalyticAdd
    BLAST
    Regioni454 – 47724LinkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG85664.

    Family and domain databases

    Gene3Di2.70.100.10. 1 hit.
    InterProiIPR000254. Cellulose-bd_dom_fun.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view]
    PfamiPF00734. CBM_1. 1 hit.
    PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view]
    PRINTSiPR00734. GLHYDRLASE7.
    ProDomiPD001821. CBD_fun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00236. fCBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 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.

    P62694-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV    50
    IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG 100
    VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV 150
    SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI 200
    NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV 250
    GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 300
    TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA 350
    EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT 400
    NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS 450
    GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT 500
    TCQVLNPYYS QCL 513
    Length:513
    Mass (Da):54,073
    Last modified:July 21, 1986 - v1
    Checksum:i9F5C0A8A854F2C12
    GO

    Sequence databases

    PIRiA00902. EUTQI.

    Cross-referencesi

    Sequence databases

    PIRi A00902. EUTQI.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AZ6 NMR - A 478-513 [» ]
    1AZH NMR - A 478-513 [» ]
    1AZJ NMR - A 478-513 [» ]
    1AZK NMR - A 478-513 [» ]
    1CBH NMR - A 478-513 [» ]
    1CEL X-ray 1.80 A/B 19-451 [» ]
    1DY4 X-ray 1.90 A 19-451 [» ]
    1EGN X-ray 1.60 A 18-451 [» ]
    1Q2B X-ray 1.60 A 18-451 [» ]
    1Q2E X-ray 1.75 A/B 19-451 [» ]
    2CBH NMR - A 478-513 [» ]
    2CEL X-ray 2.00 A/B 19-451 [» ]
    2V3I X-ray 1.05 A 19-451 [» ]
    2V3R X-ray 1.60 A 19-451 [» ]
    3CEL X-ray 2.00 A 19-451 [» ]
    4C4C X-ray 1.45 A 19-451 [» ]
    4C4D X-ray 1.32 A 19-451 [» ]
    4CEL X-ray 2.20 A/B 19-451 [» ]
    5CEL X-ray 1.90 A 19-451 [» ]
    6CEL X-ray 1.70 A 19-451 [» ]
    7CEL X-ray 1.90 A 19-451 [» ]
    8CEL model - A 18-451 [» ]
    ProteinModelPortali P62694.
    SMRi P62694. Positions 18-451, 478-513.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH7. Glycoside Hydrolase Family 7.
    mycoCLAPi CBH7A_TRIRE.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG85664.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16499.

    Miscellaneous databases

    EvolutionaryTracei P62694.

    Family and domain databases

    Gene3Di 2.70.100.10. 1 hit.
    InterProi IPR000254. Cellulose-bd_dom_fun.
    IPR008985. ConA-like_lec_gl_sf.
    IPR001722. Glyco_hydro_7.
    [Graphical view ]
    Pfami PF00734. CBM_1. 1 hit.
    PF00840. Glyco_hydro_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00734. GLHYDRLASE7.
    ProDomi PD001821. CBD_fun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00236. fCBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    SSF57180. SSF57180. 1 hit.
    PROSITEi PS00562. CBM1_1. 1 hit.
    PS51164. CBM1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma reesei strain L27."
      Shoemaker S., Schweickart V., Ladner M., Gelfand D., Kwok S., Myambo K., Innis M.
      Biotechnology (N.Y.) 1:691-696(1983)
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: L27.
    2. "Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei."
      Tomme P., Clayssens M.
      FEBS Lett. 243:239-243(1989)
      Cited for: ACTIVE SITE.
      Strain: ATCC 26921 / CBS 392.92 / QM9414.
    3. "The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei."
      Divne C., Staahlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K.C., Teeri T.T., Jones T.A.
      Science 265:524-528(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452.
    4. "High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei."
      Divne C., Staahlberg J., Teeri T.T., Jones T.A.
      J. Mol. Biol. 275:309-325(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452.
      Strain: ATCC 26921 / CBS 392.92 / QM9414.
    5. "Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing."
      Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., Gronenborn A.M.
      Biochemistry 28:7241-7257(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 478-513.
    6. "Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei."
      Mattinen M.L., Kontteli M., Kerovuo J., Linder M., Annila A., Lindeberg G., Reinikainen T., Drakenberg T.
      Protein Sci. 6:294-303(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 478-513.

    Entry informationi

    Entry nameiGUX1_HYPJE
    AccessioniPrimary (citable) accession number: P62694
    Secondary accession number(s): P00725
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.

    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