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Q06886

- GUX1_PENJA

UniProt

Q06886 - GUX1_PENJA

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Protein

Exoglucanase 1

Gene

cbh1

Organism
Penicillium janthinellum (Penicillium vitale)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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 sitei235 – 2351NucleophileBy similarity
Active sitei240 – 2401Proton 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.
mycoCLAPiCBH7A_PENJA.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiPenicillium janthinellum (Penicillium vitale)
Taxonomic identifieri5079 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 537519Exoglucanase 1PRO_0000007923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi509 ↔ 526By similarity
Disulfide bondi520 ↔ 536By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ06886.
SMRiQ06886. Positions 503-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini501 – 53737CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 453435CatalyticAdd
BLAST
Regioni454 – 47724LinkerAdd
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.

Q06886-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGSISYQIY KGALLLSALL NSVSAQQVGT LTAETHPALT WSKCTAGXCS
60 70 80 90 100
QVSGSVVIDA NWPXVHSTSG STNCYTGNTW DATLCPDDVT CAANCAVDGA
110 120 130 140 150
RRQHLRVTTS GNSLRINFVT TASQKNIGSR LYLLENDTTY QKFNLLNQEF
160 170 180 190 200
TFDVDVSNLP CGLNGALYFV DMDADGGMAK YPTNKAGAKY GTGYCDSQCP
210 220 230 240 250
RDLKFINGQA NVDGWTPSKN DVNSGIGNHG SCCAEMDIWE ANSISNAVTP
260 270 280 290 300
HPCDTPSQTM CTGQRCGGTY STDRYGGTCD PDGCDFNPYR MGVTNFYGPG
310 320 330 340 350
ETIDTKSPFT VVTQFLTNDG TSTGTLSEIK RFYVQGGKVI GNPQSTIVGV
360 370 380 390 400
SGNSITDSWC NAQKSAFGDT NEFSKHGGMA GMGAGLADGM VLVMSLWDDH
410 420 430 440 450
ASDMLWLDST YPTNATSTTP GAKRGTCDIS RRPNTVESTY PNAYVIYSNI
460 470 480 490 500
KTGPLNSTFT GGTTSSSSTT TTTSKSTSTS SSSKTTTTVT TTTTSSGSSG
510 520 530
TGARDWAQCG GNGWTGPTTC VSPYTCTKQN DWYSQCL
Length:537
Mass (Da):56,845
Last modified:February 1, 1995 - v1
Checksum:iA6B9C6EB73F17FE4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59054 mRNA. Translation: CAA41780.1.
PIRiJU0150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59054 mRNA. Translation: CAA41780.1 .
PIRi JU0150.

3D structure databases

ProteinModelPortali Q06886.
SMRi Q06886. Positions 503-537.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPi CBH7A_PENJA.

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. "Cloning, sequencing, and heterologous expression of a cellulase-encoding cDNA (cbh1) from Penicillium janthinellum."
    Koch A., Weigel C.T.O., Schulz G.
    Gene 124:57-65(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C41.

Entry informationi

Entry nameiGUX1_PENJA
AccessioniPrimary (citable) accession number: Q06886
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 79 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