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Q00548

- GUX1_CRYPA

UniProt

Q00548 - GUX1_CRYPA

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Protein

Exoglucanase 1

Gene

CBH-1

Organism
Cryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Status
Reviewed - Annotation score: 3 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 sitei230 – 2301NucleophileBy similarity
Active sitei235 – 2351Proton donorBy similarity

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17643.

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_CRYPA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase I
Beta-glucancellobiohydrolase I
Exocellobiohydrolase I
Exoglucanase I
Gene namesi
Name:CBH-1
OrganismiCryphonectria parasitica (Chesnut blight fungus) (Endothia parasitica)
Taxonomic identifieri5116 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeDiaporthalesCryphonectriaceaeCryphonectria-Endothia complexCryphonectria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 452434Exoglucanase 1PRO_0000007920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ00548.
SMRiQ00548. Positions 22-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OMAiLQSETHP.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q00548-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSKFALTGS LLAGAVNAQG VGTQQTETHP QMTWQSCTSP SSCTTNQGEV
60 70 80 90 100
VIDSNWRWVH DKDGYVNCYT GNTWNTTLCP DDKTCAANCV LDGADYSSTY
110 120 130 140 150
GITTSGNALS LQFVTQSSGK NIGSRTYLME SSTKYHLFDL IGNEFAFDVD
160 170 180 190 200
LSKLPCGLNG ALYFVTMDAD GGMAKYSTNT AGAEYGTGYC DSQCPRDLKF
210 220 230 240 250
INGQGNVEGW TPSTNDANAG VGGLGSCCSE MDVWEANSMD MAYTPHPCET
260 270 280 290 300
AAQHSCNADE CGGTYSSSRY AGDCDPDGCD WNPFRMGNKD FYGSGDTVDT
310 320 330 340 350
SQKFTVVTQF HGSGSSLTEI SQYYIQGGTK IQQPNSTWPT LTGYNSITDD
360 370 380 390 400
FCKAQKVEFN DTDVFSEKGG LAQMGAGMAD GMVLVMSLWD DHYANMLWLD
410 420 430 440 450
STYPVDADAS SPGKQRGTCA TTSGVPADVE SSDASATVIY SNIKFGPIGA

TY
Length:452
Mass (Da):48,358
Last modified:November 1, 1996 - v1
Checksum:i5802FD112C2CA864
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43048 Genomic DNA. Translation: AAB00479.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43048 Genomic DNA. Translation: AAB00479.1 .

3D structure databases

ProteinModelPortali Q00548.
SMRi Q00548. Positions 22-452.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH7. Glycoside Hydrolase Family 7.
mycoCLAPi CBH7A_CRYPA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OMAi LQSETHP.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17643.

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein-linked signaling pathway involved in fungal pathogenesis."
    Wang P., Nuss D.L.
    Proc. Natl. Acad. Sci. U.S.A. 92:11529-11533(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiGUX1_CRYPA
AccessioniPrimary (citable) accession number: Q00548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 72 of the entry and version 1 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