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P07987

- GUX2_HYPJE

UniProt

P07987 - GUX2_HYPJE

Protein

Exoglucanase 2

Gene

cbh2

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 122 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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 sitei199 – 1991
    Active sitei245 – 2451Proton donor
    Active sitei425 – 4251Nucleophile

    GO - Molecular functioni

    1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
    2. cellulose binding Source: InterPro
    3. identical protein binding Source: IntAct

    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.
    mycoCLAPiCBH6B_TRIRE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exoglucanase 2 (EC:3.2.1.91)
    Alternative name(s):
    1,4-beta-cellobiohydrolase
    Exocellobiohydrolase II
    Short name:
    CBHII
    Exoglucanase II
    Gene namesi
    Name:cbh2
    OrganismiHypocrea jecorina (Trichoderma reesei)
    Taxonomic identifieri51453 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi199 – 1991D → A: 20% of wild-type activity.
    Mutagenesisi245 – 2451D → A: No measurable activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 471447Exoglucanase 2PRO_0000007911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi34 ↔ 51By similarity
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi45 ↔ 61By similarity
    Glycosylationi111 – 1111O-linked (Man...)1 Publication
    Glycosylationi121 – 1211O-linked (Man...)1 Publication
    Glycosylationi130 – 1301O-linked (Man...)1 Publication
    Glycosylationi133 – 1331O-linked (Man...)1 Publication
    Glycosylationi134 – 1341O-linked (Man...)1 Publication
    Glycosylationi139 – 1391O-linked (Man...)1 Publication
    Glycosylationi146 – 1461O-linked (Man...)1 Publication
    Disulfide bondi200 ↔ 2591 Publication
    Glycosylationi313 – 3131N-linked (GlcNAc...)1 Publication
    Glycosylationi334 – 3341N-linked (GlcNAc...)1 Publication
    Disulfide bondi392 ↔ 4391 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-8155616,EBI-8155616

    Protein-protein interaction databases

    MINTiMINT-8401560.
    STRINGi51453.JGI72567.

    Structurei

    Secondary structure

    1
    471
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni116 – 1194
    Beta strandi120 – 1223
    Helixi126 – 13510
    Helixi137 – 1393
    Helixi142 – 15110
    Beta strandi158 – 1603
    Helixi163 – 1653
    Helixi166 – 18116
    Beta strandi186 – 1927
    Beta strandi202 – 2043
    Helixi211 – 2133
    Helixi215 – 23218
    Turni233 – 2353
    Beta strandi238 – 2425
    Beta strandi244 – 2463
    Helixi247 – 2526
    Helixi257 – 27620
    Beta strandi282 – 2876
    Helixi291 – 2944
    Helixi297 – 31317
    Beta strandi320 – 3267
    Helixi340 – 3423
    Helixi350 – 35910
    Beta strandi370 – 3745
    Beta strandi379 – 3824
    Beta strandi392 – 3965
    Beta strandi403 – 4053
    Beta strandi410 – 4167
    Beta strandi432 – 4343
    Helixi437 – 4404
    Helixi456 – 4649

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CB2X-ray2.00A/B107-471[»]
    1HGWX-ray2.10A/B107-471[»]
    1HGYX-ray2.20A/B107-471[»]
    1QJWX-ray1.90A/B107-471[»]
    1QK0X-ray2.10A/B109-471[»]
    1QK2X-ray2.00A/B109-471[»]
    3CBHX-ray2.00A107-471[»]
    4AU0X-ray1.70A/B109-471[»]
    4AX6X-ray2.30A/B109-471[»]
    4AX7X-ray1.70A/B/C/D109-471[»]
    4I5RX-ray1.50A154-331[»]
    A347-471[»]
    4I5UX-ray1.22A158-331[»]
    A425-471[»]
    ProteinModelPortaliP07987.
    SMRiP07987. Positions 29-62, 109-471.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07987.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 6237CBM1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 10641LinkerAdd
    BLAST
    Regioni107 – 471365CatalyticAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5297.
    OMAiKCANAQS.

    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.

    P07987-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST    50
    CVYSNDYYSQ CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT 100
    RVPPVGSGTA TYSGNPFVGV TPWANAYYAS EVSSLAIPSL TGAMATAAAA 150
    VAKVPSFMWL DTLDKTPLME QTLADIRTAN KNGGNYAGQF VVYDLPDRDC 200
    AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL VIEPDSLANL 250
    VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ 300
    DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE 350
    KLYIHAIGPL LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG 400
    IRPSANTGDS LLDSFVWVKP GGECDGTSDS SAPRFDSHCA LPDALQPAPQ 450
    AGAWFQAYFV QLLTNANPSF L 471
    Length:471
    Mass (Da):49,653
    Last modified:August 1, 1988 - v1
    Checksum:iC4711BC335B1BD88
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3591P → R in AAA72922. 1 PublicationCurated
    Sequence conflicti449 – 4491P → A in AAA72922. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16190 Genomic DNA. Translation: AAA34210.1.
    M55080 Genomic DNA. Translation: AAA72922.1.
    PIRiA26160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16190 Genomic DNA. Translation: AAA34210.1 .
    M55080 Genomic DNA. Translation: AAA72922.1 .
    PIRi A26160.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CB2 X-ray 2.00 A/B 107-471 [» ]
    1HGW X-ray 2.10 A/B 107-471 [» ]
    1HGY X-ray 2.20 A/B 107-471 [» ]
    1QJW X-ray 1.90 A/B 107-471 [» ]
    1QK0 X-ray 2.10 A/B 109-471 [» ]
    1QK2 X-ray 2.00 A/B 109-471 [» ]
    3CBH X-ray 2.00 A 107-471 [» ]
    4AU0 X-ray 1.70 A/B 109-471 [» ]
    4AX6 X-ray 2.30 A/B 109-471 [» ]
    4AX7 X-ray 1.70 A/B/C/D 109-471 [» ]
    4I5R X-ray 1.50 A 154-331 [» ]
    A 347-471 [» ]
    4I5U X-ray 1.22 A 158-331 [» ]
    A 425-471 [» ]
    ProteinModelPortali P07987.
    SMRi P07987. Positions 29-62, 109-471.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-8401560.
    STRINGi 51453.JGI72567.

    Protein family/group databases

    CAZyi CBM1. Carbohydrate-Binding Module Family 1.
    GH6. Glycoside Hydrolase Family 6.
    mycoCLAPi CBH6B_TRIRE.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5297.
    OMAi KCANAQS.

    Miscellaneous databases

    EvolutionaryTracei P07987.

    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. "Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II."
      Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J.
      Gene 51:43-52(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: VTT-D-80133.
    2. "Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei."
      Chen C.M., Gritzali M., Stafford D.W.
      Biotechnology (N.Y.) 5:274-278(1987)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26921 / CBS 392.92 / QM9414.
    3. "The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414."
      Faegerstam L.G., Pettersson L.G.
      FEBS Lett. 119:97-100(1980)
      Cited for: PROTEIN SEQUENCE OF 25-44.
      Strain: ATCC 26921 / CBS 392.92 / QM9414.
    4. "Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei."
      Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A.
      Science 249:380-386(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    5. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139; THR-146; ASN-313 AND ASN-334.

    Entry informationi

    Entry nameiGUX2_HYPJE
    AccessioniPrimary (citable) accession number: P07987
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 122 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, Direct protein sequencing

    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