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Q9P8P3

- GUX1_TRIHA

UniProt

Q9P8P3 - GUX1_TRIHA

Protein

Exoglucanase 1

Gene

cbh1

Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 sitei139 – 1391By similarity
    Active sitei225 – 2251NucleophileBy similarity
    Active sitei230 – 2301Proton donorBy similarity

    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.
    GH7. Glycoside Hydrolase Family 7.

    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
    OrganismiTrichoderma harzianum (Hypocrea lixii)
    Taxonomic identifieri5544 [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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 505488Exoglucanase 1PRO_0000007925Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Pyrrolidone carboxylic acidBy similarity
    Disulfide bondi21 ↔ 88By similarity
    Disulfide bondi36 ↔ 41By similarity
    Disulfide bondi66 ↔ 87By similarity
    Disulfide bondi77 ↔ 83By similarity
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi151 ↔ 410By similarity
    Disulfide bondi185 ↔ 223By similarity
    Disulfide bondi189 ↔ 222By similarity
    Disulfide bondi243 ↔ 269By similarity
    Disulfide bondi251 ↔ 256By similarity
    Disulfide bondi274 ↔ 344By similarity
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi477 ↔ 494By similarity
    Disulfide bondi488 ↔ 504By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    PRIDEiQ9P8P3.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 378
    Beta strandi40 – 5011
    Helixi52 – 543
    Beta strandi57 – 593
    Beta strandi65 – 684
    Turni74 – 763
    Helixi80 – 867
    Beta strandi87 – 893
    Helixi94 – 985
    Beta strandi100 – 1034
    Beta strandi106 – 1138
    Beta strandi119 – 1268
    Beta strandi138 – 1458
    Beta strandi154 – 1607
    Turni164 – 1707
    Helixi177 – 1804
    Beta strandi194 – 1963
    Beta strandi218 – 2225
    Beta strandi225 – 2317
    Beta strandi236 – 2416
    Beta strandi243 – 2475
    Beta strandi249 – 2524
    Helixi253 – 2564
    Beta strandi258 – 2625
    Beta strandi266 – 2694
    Turni278 – 2825
    Beta strandi286 – 2905
    Beta strandi293 – 2964
    Beta strandi301 – 3077
    Beta strandi313 – 3197
    Beta strandi322 – 3254
    Beta strandi329 – 3313
    Beta strandi334 – 3407
    Helixi341 – 35111
    Helixi355 – 3584
    Helixi361 – 37010
    Beta strandi373 – 3808
    Turni383 – 3875
    Helixi388 – 3914
    Beta strandi408 – 4103
    Turni412 – 4154
    Helixi417 – 4237
    Beta strandi428 – 43811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y9NX-ray2.89A19-449[»]
    2YOKX-ray1.67A19-443[»]
    ProteinModelPortaliQ9P8P3.
    SMRiQ9P8P3. Positions 18-447, 470-505.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini469 – 50537CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 449432CatalyticAdd
    BLAST
    Regioni450 – 46920LinkerAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

    Q9P8P3-1 [UniParc]FASTAAdd to Basket

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    MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL    50
    DANWRWTHDT KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV 100
    TTSGDALTLQ FVTASNVGSR LYLMANDSTY QEFTLSGNEF SFDVDVSQLP 150
    CGLNGALYFV SMDADGGQSK YPGNAAGAKY GTGYCDSQCP RDLKFINGQA 200
    NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP HPCETVGQTM 250
    CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK 300
    LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA 350
    FGGTSFTDKG GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA 400
    STPGAKRGSC STSSGVPAQV EAQSPNSKVI YSNIRFGPIG STGGNTGSNP 450
    PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT GWTGPTRCAS GYTCQVLNPF 500
    YSQCL 505
    Length:505
    Mass (Da):53,216
    Last modified:October 1, 2000 - v1
    Checksum:i52930722F97D7BF0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF223252 Genomic DNA. Translation: AAF36391.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF223252 Genomic DNA. Translation: AAF36391.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y9N X-ray 2.89 A 19-449 [» ]
    2YOK X-ray 1.67 A 19-443 [» ]
    ProteinModelPortali Q9P8P3.
    SMRi Q9P8P3. Positions 18-447, 470-505.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    PRIDEi Q9P8P3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Cloning and sequencing of a cellobiohydrolase gene from Trichoderma harzianum FP 108."
      Guilfoile P.G., Burns R., Gu Z.-Y., Amundson M., Chang F.-H.
      J. Minn. Acad. Sci. 64:18-22(1999)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FP 108.

    Entry informationi

    Entry nameiGUX1_TRIHA
    AccessioniPrimary (citable) accession number: Q9P8P3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 63 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