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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 – 1391By similarity
Active sitei225 – 2251NucleophileBy similarity
Active sitei230 – 2301Proton donorBy 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 505488Exoglucanase 1PRO_0000007925Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ9P8P3.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 378Combined sources
Beta strandi40 – 5011Combined sources
Helixi52 – 543Combined sources
Beta strandi57 – 593Combined sources
Beta strandi65 – 684Combined sources
Turni74 – 763Combined sources
Helixi80 – 867Combined sources
Beta strandi87 – 893Combined sources
Helixi94 – 985Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi138 – 1458Combined sources
Beta strandi154 – 1607Combined sources
Turni164 – 1707Combined sources
Helixi177 – 1804Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi218 – 2225Combined sources
Beta strandi225 – 2317Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi243 – 2475Combined sources
Beta strandi249 – 2524Combined sources
Helixi253 – 2564Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi266 – 2694Combined sources
Turni278 – 2825Combined sources
Beta strandi286 – 2905Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi301 – 3077Combined sources
Beta strandi313 – 3197Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi334 – 3407Combined sources
Helixi341 – 35111Combined sources
Helixi355 – 3584Combined sources
Helixi361 – 37010Combined sources
Beta strandi373 – 3808Combined sources
Turni383 – 3875Combined sources
Helixi388 – 3914Combined sources
Beta strandi408 – 4103Combined sources
Turni412 – 4154Combined sources
Helixi417 – 4237Combined sources
Beta strandi428 – 43811Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini469 – 50537CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 449432CatalyticAdd
BLAST
Regioni450 – 46920LinkerAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
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

« 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:
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.
IPR013320. ConA-like_dom.
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: October 29, 2014
This is version 64 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