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P19355

- GUX1_HYPRU

UniProt

P19355 - GUX1_HYPRU

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Protein

Exoglucanase 1

Gene

cbh1

Organism
Hypocrea rufa (Trichoderma viride)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 sitei229 – 2291NucleophileBy similarity
Active sitei234 – 2341Proton 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
Complete GO annotation...

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
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiHypocrea rufa (Trichoderma viride)
Taxonomic identifieri5547 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 514497Exoglucanase 1PRO_0000007928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 89By similarity
Disulfide bondi36 ↔ 42By similarity
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi67 ↔ 88By similarity
Disulfide bondi78 ↔ 84By similarity
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi155 ↔ 414By similarity
Disulfide bondi189 ↔ 227By similarity
Disulfide bondi193 ↔ 226By similarity
Disulfide bondi247 ↔ 273By similarity
Disulfide bondi255 ↔ 260By similarity
Disulfide bondi278 ↔ 348By similarity
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi486 ↔ 503By similarity
Disulfide bondi497 ↔ 513By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP19355.
SMRiP19355. Positions 18-451, 479-514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini478 – 51437CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 453436CatalyticAdd
BLAST
Regioni454 – 47825LinkerAdd
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.
IPR013320. ConA-like_dom.
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.

P19355-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYQKLALISA FLATARAQSA CTLQAETHPP LTWQKCSSGG TCTQQTGSVV
60 70 80 90 100
IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG
110 120 130 140 150
VTTSADSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV
160 170 180 190 200
SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI
210 220 230 240 250
NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV
260 270 280 290 300
GQEICDGDSC GGTYSGDRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
310 320 330 340 350
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGDYSG NSLDDDYCAA
360 370 380 390 400
EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT
410 420 430 440 450
NETSSTPGAV RGSCSTSSGV PAQLESNSPN AKVVYSNIKF GPIGSTGNSS
460 470 480 490 500
GGNPPGGNPP GTTTTRRPAT STGSSPGPTQ THYGQCGGIG YSGPTVCASG
510
STCQVLNPYY SQCL
Length:514
Mass (Da):54,002
Last modified:July 19, 2004 - v2
Checksum:iC5B1FB734C9CDAF5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731S → T in CAA37878. (PubMed:2216737)Curated
Sequence conflicti256 – 2561D → E in CAA37878. (PubMed:2216737)Curated
Sequence conflicti401 – 4011N → D in CAA37878. (PubMed:2216737)Curated
Sequence conflicti414 – 4141C → S in CAA37878. (PubMed:2216737)Curated
Sequence conflicti449 – 4491S → P in CAA37878. (PubMed:2216737)Curated
Sequence conflicti462 – 4621Missing(PubMed:2216737)Curated
Sequence conflicti466 – 4661R → P(PubMed:2216737)Curated
Sequence conflicti492 – 4921S → I in CAA37878. (PubMed:2216737)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53931 Genomic DNA. Translation: CAA37878.1.
AB021656 Genomic DNA. Translation: BAA36215.1.
PIRiS11439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53931 Genomic DNA. Translation: CAA37878.1 .
AB021656 Genomic DNA. Translation: BAA36215.1 .
PIRi S11439.

3D structure databases

ProteinModelPortali P19355.
SMRi P19355. Positions 18-451, 479-514.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

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.
IPR013320. ConA-like_dom.
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. "Nucleotide sequence of the cellobiohydrolase gene from Trichoderma viride."
    Cheng C., Tsukagoshi N., Udaka S.
    Nucleic Acids Res. 18:5559-5559(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Watanabe M.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MC300-1.

Entry informationi

Entry nameiGUX1_HYPRU
AccessioniPrimary (citable) accession number: P19355
Secondary accession number(s): O93832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3