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Protein

Exoglucanase 1

Gene

CEL1

Organism
Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola)
Status
Reviewed-Annotation score: 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 disaccharide 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)DescriptionActionsGraphical viewLength
Active sitei232NucleophileBy similarity1
Active sitei237Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.

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:CEL1
OrganismiCochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola)
Taxonomic identifieri5017 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeBipolaris

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000791919 – 456Exoglucanase 1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Glycosylationi47N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ00328.

Structurei

3D structure databases

ProteinModelPortaliQ00328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
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.

Q00328-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRTLAFASL SLYGAARAQQ VGTSTAENHP KLTWQTCTGT GGTNCSNKSG
60 70 80 90 100
SVVLDSNWRW AHNVGGYTNC YTGNSWSTQY CPDGDSCTKN CAIDGADYSG
110 120 130 140 150
TYGITTSNNA LSLKFVTKGS FSSNIGSRTY LMETDTKYQM FNLINKEFTF
160 170 180 190 200
DVDVSKLPCG LNGALYFVEM AADGGIGKGN NKAGAKYGTG YCDSQCPHDI
210 220 230 240 250
KFINGKANVE GWNPSDADPN GGAGKIGACC PEMDIWEANS ISTAYTPHPC
260 270 280 290 300
RGVGLQECSD AASCGDGSNR YDGQCDKDGC DFNSYRMGVK DFYGPGATLD
310 320 330 340 350
TTKKMTVITQ FLGSGSSLSE IKRFYVQNGK VYKNSQSAVA GVTGNSITES
360 370 380 390 400
FCTAQKKAFG DTSSFAALGG LNEMGASLAR GHVLIMSLWG DHAVNMLWLD
410 420 430 440 450
STYPTDADPS KPGAARGTCP TTSGKPEDVE KNSPDATVVF SNIKFGPIGS

TFAQPA
Length:456
Mass (Da):48,304
Last modified:November 1, 1996 - v1
Checksum:i8014094907DEEA52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25129 Genomic DNA. Translation: AAC49089.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25129 Genomic DNA. Translation: AAC49089.1.

3D structure databases

ProteinModelPortaliQ00328.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.

Proteomic databases

PRIDEiQ00328.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiGUX1_COCCA
AccessioniPrimary (citable) accession number: Q00328
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 76 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.