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Q92400

- GUX2_AGABI

UniProt

Q92400 - GUX2_AGABI

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Protein

Exoglucanase

Gene
cel2
Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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 sitei227 – 2271Nucleophile By similarity
Active sitei232 – 2321Proton donor By 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 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Beta-glucancellobiohydrolase
Exocellobiohydrolase
Gene namesi
Name:cel2
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

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 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 506488ExoglucanasePRO_0000007917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi308 – 3081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi447 – 4471N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi478 ↔ 495 By similarity
Disulfide bondi489 ↔ 505 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ92400.

Structurei

3D structure databases

ProteinModelPortaliQ92400.
SMRiQ92400. Positions 19-451, 472-506.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini470 – 50637CBM1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 450432CatalyticAdd
BLAST
Regioni451 – 47323LinkerAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OMAiRGTCSRD.

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.

Q92400-1 [UniParc]FASTAAdd to Basket

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MFPRSILLAL SLTAVALGQQ VGTNMAENHP SLTWQRCTSS GCQNVNGKVT    50
LDANWRWTHR INDFTNCYTG NEWDTSICPD GVTCAENCAL DGADYAGTYG 100
VTSSGTALTL KFVTESQQKN IGSRLYLMAD DSNYEIFNLL NKEFTFDVDV 150
SKLPCGLNGA LYFSEMAADG GMSSTNTAGA KYGTGYCDSQ CPRDIKFIDG 200
EANSEGWEGS PNDVNAGTGN FGACCGEMDI WEANSISSAY TPHPCREPGL 250
QRCEGNTCSV NDRYATECDP DGCDFNSFRM GDKSFYGPGM TVDTNQPITV 300
VTQFITDNGS DNGNLQEIRR IYVQNGQVIQ NSNVNIPGID SGNSISAEFC 350
DQAKEAFGDE RSFQDRGGLS GMGSALDRGM VLVLSIWDDH AVNMLWLDSD 400
YPLDASPSQP GISRGTCSRD SGKPEDVEAN AGGVQVVYSN IKFGDINSTF 450
NNNGGGGGNP SPTTTRPNSP AQTMWGQCGG QGWTGPTACQ SPSTCHVIND 500
FYSQCF 506
Length:506
Mass (Da):54,320
Last modified:February 1, 1997 - v1
Checksum:i0D0390CA4E71BC55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z50094 mRNA. Translation: CAA90422.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z50094 mRNA. Translation: CAA90422.1 .

3D structure databases

ProteinModelPortali Q92400.
SMRi Q92400. Positions 19-451, 472-506.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

Proteomic databases

PRIDEi Q92400.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OMAi RGTCSRD.

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. "Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with similarity to fungal cellobiohydrolase I and beta-mannanase, respectively, is regulated by the carbon source."
    Yague E., Mehak-Zunic M., Morgan L., Wood D.A., Thurston C.F.
    Microbiology 143:239-244(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: D649.

Entry informationi

Entry nameiGUX2_AGABI
AccessioniPrimary (citable) accession number: Q92400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: October 16, 2013
This is version 73 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

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