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Q9P8P3

- GUX1_TRIHA

UniProt

Q9P8P3 - GUX1_TRIHA

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Protein
Exoglucanase 1
Gene
cbh1
Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed - Annotation score: 4 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 sitei139 – 1391 By similarity
Active sitei225 – 2251Nucleophile By similarity
Active sitei230 – 2301Proton donor By 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 505488Exoglucanase 1
PRO_0000007925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Pyrrolidone carboxylic acid By similarity
Disulfide bondi21 ↔ 88 By similarity
Disulfide bondi36 ↔ 41 By similarity
Disulfide bondi66 ↔ 87 By similarity
Disulfide bondi77 ↔ 83 By similarity
Glycosylationi93 – 931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi126 – 1261N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi151 ↔ 410 By similarity
Disulfide bondi185 ↔ 223 By similarity
Disulfide bondi189 ↔ 222 By similarity
Disulfide bondi243 ↔ 269 By similarity
Disulfide bondi251 ↔ 256 By similarity
Disulfide bondi274 ↔ 344 By similarity
Glycosylationi283 – 2831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi397 – 3971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi477 ↔ 494 By similarity
Disulfide bondi488 ↔ 504 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ9P8P3.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 378
Beta strandi40 – 5011
Helixi52 – 543
Beta strandi57 – 593
Beta strandi65 – 684
Turni74 – 763
Helixi80 – 867
Beta strandi87 – 893
Helixi94 – 985
Beta strandi100 – 1034
Beta strandi106 – 1138
Beta strandi119 – 1268
Beta strandi138 – 1458
Beta strandi154 – 1607
Turni164 – 1707
Helixi177 – 1804
Beta strandi194 – 1963
Beta strandi218 – 2225
Beta strandi225 – 2317
Beta strandi236 – 2416
Beta strandi243 – 2475
Beta strandi249 – 2524
Helixi253 – 2564
Beta strandi258 – 2625
Beta strandi266 – 2694
Turni278 – 2825
Beta strandi286 – 2905
Beta strandi293 – 2964
Beta strandi301 – 3077
Beta strandi313 – 3197
Beta strandi322 – 3254
Beta strandi329 – 3313
Beta strandi334 – 3407
Helixi341 – 35111
Helixi355 – 3584
Helixi361 – 37010
Beta strandi373 – 3808
Turni383 – 3875
Helixi388 – 3914
Beta strandi408 – 4103
Turni412 – 4154
Helixi417 – 4237
Beta strandi428 – 43811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y9NX-ray2.89A19-449[»]
2YOKX-ray1.67A19-443[»]
ProteinModelPortaliQ9P8P3.
SMRiQ9P8P3. Positions 18-447, 470-505.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini469 – 50537CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 449432Catalytic
Add
BLAST
Regioni450 – 46920Linker
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
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.

Q9P8P3-1 [UniParc]FASTAAdd to Basket

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MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL    50
DANWRWTHDT KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV 100
TTSGDALTLQ FVTASNVGSR LYLMANDSTY QEFTLSGNEF SFDVDVSQLP 150
CGLNGALYFV SMDADGGQSK YPGNAAGAKY GTGYCDSQCP RDLKFINGQA 200
NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP HPCETVGQTM 250
CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK 300
LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA 350
FGGTSFTDKG GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA 400
STPGAKRGSC STSSGVPAQV EAQSPNSKVI YSNIRFGPIG STGGNTGSNP 450
PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT GWTGPTRCAS GYTCQVLNPF 500
YSQCL 505
Length:505
Mass (Da):53,216
Last modified:October 1, 2000 - v1
Checksum:i52930722F97D7BF0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF223252 Genomic DNA. Translation: AAF36391.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF223252 Genomic DNA. Translation: AAF36391.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Y9N X-ray 2.89 A 19-449 [» ]
2YOK X-ray 1.67 A 19-443 [» ]
ProteinModelPortali Q9P8P3.
SMRi Q9P8P3. Positions 18-447, 470-505.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

Proteomic databases

PRIDEi Q9P8P3.

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.
IPR008985. ConA-like_lec_gl_sf.
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 and sequencing of a cellobiohydrolase gene from Trichoderma harzianum FP 108."
    Guilfoile P.G., Burns R., Gu Z.-Y., Amundson M., Chang F.-H.
    J. Minn. Acad. Sci. 64:18-22(1999)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FP 108.

Entry informationi

Entry nameiGUX1_TRIHA
AccessioniPrimary (citable) accession number: Q9P8P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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

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