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Protein

Exoglucanase 1

Gene

cbh1

Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:21876370). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).Curated1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.2 Publications

Kineticsi

kcat is 23.2 min(-1) with p-nitrophenyl-D-cellobioside as substrate and 44.6 min(-1) with 2-chloro-4-nitrophenyl-beta-lactoside as substrate.1 Publication
  1. KM=3.4 mM for p-nitrophenyl-D-cellobioside1 Publication
  2. KM=3.7 mM for 2-chloro-4-nitrophenyl-beta-lactoside1 Publication
  1. Vmax=0.016 mmol/min/mg enzyme for p-nitrophenyl-D-cellobioside1 Publication
  2. Vmax=0.031 mmol/min/mg enzyme for 2-chloro-4-nitrophenyl-beta-lactoside1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei225Nucleophile1 Publication1
Active sitei230Proton donor/acceptor1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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
Cellobiohydrolase 7A
Short name:
Cel7A
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000000792518 – 505Exoglucanase 1Add BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi21 ↔ 881 Publication
Disulfide bondi36 ↔ 411 Publication
Disulfide bondi66 ↔ 871 Publication
Disulfide bondi77 ↔ 831 Publication
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi151 ↔ 4101 Publication
Disulfide bondi185 ↔ 2231 Publication
Disulfide bondi189 ↔ 2221 Publication
Disulfide bondi243 ↔ 2691 Publication
Disulfide bondi251 ↔ 2561 Publication
Disulfide bondi274 ↔ 3441 Publication
Glycosylationi283N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi397N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

O-glycosylated. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ9P8P3

Structurei

Secondary structure

1505
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9P8P3
SMRiQ9P8P3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini469 – 505CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 449Catalytic1 PublicationAdd BLAST432
Regioni450 – 468LinkerCuratedAdd BLAST19

Domaini

The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999 GH7_CBH_EG, 1 hit
Gene3Di2.70.100.10, 1 hit
InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF00840 Glyco_hydro_7, 1 hit
PRINTSiPR00734 GLHYDRLASE7
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821 CBD_fun, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q9P8P3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL
60 70 80 90 100
DANWRWTHDT KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV
110 120 130 140 150
TTSGDALTLQ FVTASNVGSR LYLMANDSTY QEFTLSGNEF SFDVDVSQLP
160 170 180 190 200
CGLNGALYFV SMDADGGQSK YPGNAAGAKY GTGYCDSQCP RDLKFINGQA
210 220 230 240 250
NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP HPCETVGQTM
260 270 280 290 300
CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK
310 320 330 340 350
LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA
360 370 380 390 400
FGGTSFTDKG GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA
410 420 430 440 450
STPGAKRGSC STSSGVPAQV EAQSPNSKVI YSNIRFGPIG STGGNTGSNP
460 470 480 490 500
PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT GWTGPTRCAS GYTCQVLNPF

YSQCL
Length:505
Mass (Da):53,216
Last modified:October 1, 2000 - v1
Checksum:i52930722F97D7BF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF223252 Genomic DNA Translation: AAF36391.1

Similar proteinsi

Entry informationi

Entry nameiGUX1_TRIHA
AccessioniPrimary (citable) accession number: Q9P8P3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: December 20, 2017
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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