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P07987

- GUX2_HYPJE

UniProt

P07987 - GUX2_HYPJE

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Protein

Exoglucanase 2

Gene

cbh2

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - 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 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 sitei199 – 1991
Active sitei245 – 2451Proton donor
Active sitei425 – 4251Nucleophile

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro
  3. identical protein binding Source: IntAct

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.
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

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991D → A: 20% of wild-type activity.
Mutagenesisi245 – 2451D → A: No measurable activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 471447Exoglucanase 2PRO_0000007911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 51By similarity
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi45 ↔ 61By similarity
Glycosylationi111 – 1111O-linked (Man...)1 Publication
Glycosylationi121 – 1211O-linked (Man...)1 Publication
Glycosylationi130 – 1301O-linked (Man...)1 Publication
Glycosylationi133 – 1331O-linked (Man...)1 Publication
Glycosylationi134 – 1341O-linked (Man...)1 Publication
Glycosylationi139 – 1391O-linked (Man...)1 Publication
Glycosylationi146 – 1461O-linked (Man...)1 Publication
Disulfide bondi200 ↔ 2591 Publication
Glycosylationi313 – 3131N-linked (GlcNAc...)1 Publication
Glycosylationi334 – 3341N-linked (GlcNAc...)1 Publication
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

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni116 – 1194
Beta strandi120 – 1223
Helixi126 – 13510
Helixi137 – 1393
Helixi142 – 15110
Beta strandi158 – 1603
Helixi163 – 1653
Helixi166 – 18116
Beta strandi186 – 1927
Beta strandi202 – 2043
Helixi211 – 2133
Helixi215 – 23218
Turni233 – 2353
Beta strandi238 – 2425
Beta strandi244 – 2463
Helixi247 – 2526
Helixi257 – 27620
Beta strandi282 – 2876
Helixi291 – 2944
Helixi297 – 31317
Beta strandi320 – 3267
Helixi340 – 3423
Helixi350 – 35910
Beta strandi370 – 3745
Beta strandi379 – 3824
Beta strandi392 – 3965
Beta strandi403 – 4053
Beta strandi410 – 4167
Beta strandi432 – 4343
Helixi437 – 4404
Helixi456 – 4649

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray1.50A207-358[»]
A385-389[»]
A425-471[»]
4I5UX-ray1.22A369-423[»]
A425-471[»]
ProteinModelPortaliP07987.
SMRiP07987. Positions 29-62, 109-471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6237CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 10641LinkerAdd
BLAST
Regioni107 – 471365CatalyticAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5297.
OMAiKCANAQS.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591P → R in AAA72922. 1 PublicationCurated
Sequence conflicti449 – 4491P → A in AAA72922. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16190 Genomic DNA. Translation: AAA34210.1.
M55080 Genomic DNA. Translation: AAA72922.1.
PIRiA26160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M16190 Genomic DNA. Translation: AAA34210.1 .
M55080 Genomic DNA. Translation: AAA72922.1 .
PIRi A26160.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CB2 X-ray 2.00 A/B 107-471 [» ]
1HGW X-ray 2.10 A/B 107-471 [» ]
1HGY X-ray 2.20 A/B 107-471 [» ]
1QJW X-ray 1.90 A/B 107-471 [» ]
1QK0 X-ray 2.10 A/B 109-471 [» ]
1QK2 X-ray 2.00 A/B 109-471 [» ]
3CBH X-ray 2.00 A 107-471 [» ]
4AU0 X-ray 1.70 A/B 109-471 [» ]
4AX6 X-ray 2.30 A/B 109-471 [» ]
4AX7 X-ray 1.70 A/B/C/D 109-471 [» ]
4I5R X-ray 1.50 A 207-358 [» ]
A 385-389 [» ]
A 425-471 [» ]
4I5U X-ray 1.22 A 369-423 [» ]
A 425-471 [» ]
ProteinModelPortali P07987.
SMRi P07987. Positions 29-62, 109-471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-8401560.
STRINGi 51453.JGI72567.

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH6. Glycoside Hydrolase Family 6.
mycoCLAPi CBH6B_TRIRE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5297.
OMAi KCANAQS.

Miscellaneous databases

EvolutionaryTracei P07987.

Family and domain databases

Gene3Di 3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSi PR00733. GLHYDRLASE6.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Homologous domains in Trichoderma reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II."
    Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J.
    Gene 51:43-52(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: VTT-D-80133.
  2. "Nucleotide sequence and deduced primary structure of cellobiohydrolase II from Trichoderma reesei."
    Chen C.M., Gritzali M., Stafford D.W.
    Biotechnology (N.Y.) 5:274-278(1987)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26921 / CBS 392.92 / QM9414.
  3. "The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414."
    Faegerstam L.G., Pettersson L.G.
    FEBS Lett. 119:97-100(1980)
    Cited for: PROTEIN SEQUENCE OF 25-44.
    Strain: ATCC 26921 / CBS 392.92 / QM9414.
  4. "Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei."
    Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A.
    Science 249:380-386(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139; THR-146; ASN-313 AND ASN-334.

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: October 29, 2014
This is version 123 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

External Data

Dasty 3