Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Exoglucanase 2

Gene

cbh2

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 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 sitei1991
Active sitei245Proton donor1
Active sitei425Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.91. 6451.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6B_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 2 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase II
Short name:
CBHII
Exoglucanase II
Gene namesi
Name:cbh2
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi199D → A: 20% of wild-type activity. 1
Mutagenesisi245D → A: No measurable activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000000791125 – 471Exoglucanase 2Add BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34 ↔ 51By similarity
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi45 ↔ 61By similarity
Glycosylationi111O-linked (Man...)1 Publication1
Glycosylationi121O-linked (Man...)1 Publication1
Glycosylationi130O-linked (Man...)1 Publication1
Glycosylationi133O-linked (Man...)1 Publication1
Glycosylationi134O-linked (Man...)1 Publication1
Glycosylationi139O-linked (Man...)1 Publication1
Glycosylationi146O-linked (Man...)1 Publication1
Disulfide bondi200 ↔ 2591 Publication
Glycosylationi313N-linked (GlcNAc...)1 Publication1
Glycosylationi334N-linked (GlcNAc...)1 Publication1
Disulfide bondi392 ↔ 4391 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-8155616,EBI-8155616

Protein-protein interaction databases

MINTiMINT-8401560.
STRINGi51453.JGI72567.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni116 – 119Combined sources4
Beta strandi120 – 122Combined sources3
Helixi126 – 135Combined sources10
Helixi137 – 139Combined sources3
Helixi142 – 151Combined sources10
Beta strandi158 – 160Combined sources3
Helixi163 – 165Combined sources3
Helixi166 – 181Combined sources16
Beta strandi186 – 192Combined sources7
Beta strandi202 – 204Combined sources3
Helixi211 – 213Combined sources3
Helixi215 – 232Combined sources18
Turni233 – 235Combined sources3
Beta strandi238 – 242Combined sources5
Beta strandi244 – 246Combined sources3
Helixi247 – 252Combined sources6
Helixi257 – 276Combined sources20
Beta strandi282 – 287Combined sources6
Helixi291 – 294Combined sources4
Helixi297 – 313Combined sources17
Beta strandi320 – 326Combined sources7
Helixi340 – 342Combined sources3
Helixi350 – 363Combined sources14
Beta strandi370 – 374Combined sources5
Beta strandi379 – 382Combined sources4
Beta strandi392 – 396Combined sources5
Beta strandi403 – 405Combined sources3
Beta strandi410 – 416Combined sources7
Beta strandi432 – 434Combined sources3
Helixi437 – 440Combined sources4
Helixi456 – 464Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CB2X-ray2.00A/B107-471[»]
1HGWX-ray2.10A/B107-471[»]
1HGYX-ray2.20A/B107-471[»]
1QJWX-ray1.90A/B107-471[»]
1QK0X-ray2.10A/B109-471[»]
1QK2X-ray2.00A/B109-471[»]
3CBHX-ray2.00A107-471[»]
4AU0X-ray1.70A/B109-471[»]
4AX6X-ray2.30A/B109-471[»]
4AX7X-ray1.70A/B/C/D109-471[»]
4I5RX-ray1.50A158-331[»]
A425-471[»]
4I5UX-ray1.22A158-331[»]
A425-471[»]
ProteinModelPortaliP07987.
SMRiP07987.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 62CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni66 – 106LinkerAdd BLAST41
Regioni107 – 471CatalyticAdd BLAST365

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IEPE. Eukaryota.
COG5297. LUCA.
OMAiGQQAWGD.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST
60 70 80 90 100
CVYSNDYYSQ CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT
110 120 130 140 150
RVPPVGSGTA TYSGNPFVGV TPWANAYYAS EVSSLAIPSL TGAMATAAAA
160 170 180 190 200
VAKVPSFMWL DTLDKTPLME QTLADIRTAN KNGGNYAGQF VVYDLPDRDC
210 220 230 240 250
AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL VIEPDSLANL
260 270 280 290 300
VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ
310 320 330 340 350
DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE
360 370 380 390 400
KLYIHAIGPL LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG
410 420 430 440 450
IRPSANTGDS LLDSFVWVKP GGECDGTSDS SAPRFDSHCA LPDALQPAPQ
460 470
AGAWFQAYFV QLLTNANPSF L
Length:471
Mass (Da):49,653
Last modified:August 1, 1988 - v1
Checksum:iC4711BC335B1BD88
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti359P → R in AAA72922 (Ref. 2) Curated1
Sequence conflicti449P → A in AAA72922 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16190 Genomic DNA. Translation: AAA34210.1.
M55080 Genomic DNA. Translation: AAA72922.1.
PIRiA26160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16190 Genomic DNA. Translation: AAA34210.1.
M55080 Genomic DNA. Translation: AAA72922.1.
PIRiA26160.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CB2X-ray2.00A/B107-471[»]
1HGWX-ray2.10A/B107-471[»]
1HGYX-ray2.20A/B107-471[»]
1QJWX-ray1.90A/B107-471[»]
1QK0X-ray2.10A/B109-471[»]
1QK2X-ray2.00A/B109-471[»]
3CBHX-ray2.00A107-471[»]
4AU0X-ray1.70A/B109-471[»]
4AX6X-ray2.30A/B109-471[»]
4AX7X-ray1.70A/B/C/D109-471[»]
4I5RX-ray1.50A158-331[»]
A425-471[»]
4I5UX-ray1.22A158-331[»]
A425-471[»]
ProteinModelPortaliP07987.
SMRiP07987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8401560.
STRINGi51453.JGI72567.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPiCBH6B_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IEPE. Eukaryota.
COG5297. LUCA.
OMAiGQQAWGD.

Enzyme and pathway databases

BRENDAi3.2.1.91. 6451.

Miscellaneous databases

EvolutionaryTraceiP07987.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUX2_HYPJE
AccessioniPrimary (citable) accession number: P07987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 30, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.