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Protein

Exoglucanase 1

Gene

cbh1

Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed-Annotation score: 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 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 sitei139By similarity1
Active sitei225NucleophileBy similarity1
Active sitei230Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

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 acidBy similarity1
Disulfide bondi21 ↔ 88By similarity
Disulfide bondi36 ↔ 41By similarity
Disulfide bondi66 ↔ 87By similarity
Disulfide bondi77 ↔ 83By similarity
Glycosylationi93N-linked (GlcNAc...)Sequence analysis1
Glycosylationi126N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi151 ↔ 410By similarity
Disulfide bondi185 ↔ 223By similarity
Disulfide bondi189 ↔ 222By similarity
Disulfide bondi243 ↔ 269By similarity
Disulfide bondi251 ↔ 256By similarity
Disulfide bondi274 ↔ 344By similarity
Glycosylationi283N-linked (GlcNAc...)Sequence analysis1
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi477 ↔ 494By similarity
Disulfide bondi488 ↔ 504By 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 37Combined sources8
Beta strandi40 – 50Combined sources11
Helixi52 – 54Combined sources3
Beta strandi57 – 59Combined sources3
Beta strandi65 – 68Combined sources4
Turni74 – 76Combined sources3
Helixi80 – 86Combined sources7
Beta strandi87 – 89Combined sources3
Helixi94 – 98Combined sources5
Beta strandi100 – 103Combined sources4
Beta strandi106 – 113Combined sources8
Beta strandi119 – 126Combined sources8
Beta strandi138 – 145Combined sources8
Beta strandi154 – 160Combined sources7
Turni164 – 170Combined sources7
Helixi177 – 180Combined sources4
Beta strandi194 – 196Combined sources3
Beta strandi218 – 222Combined sources5
Beta strandi225 – 231Combined sources7
Beta strandi236 – 241Combined sources6
Beta strandi243 – 247Combined sources5
Beta strandi249 – 252Combined sources4
Helixi253 – 256Combined sources4
Beta strandi258 – 262Combined sources5
Beta strandi266 – 269Combined sources4
Turni278 – 282Combined sources5
Beta strandi286 – 290Combined sources5
Beta strandi293 – 296Combined sources4
Beta strandi301 – 307Combined sources7
Beta strandi313 – 319Combined sources7
Beta strandi322 – 325Combined sources4
Beta strandi329 – 331Combined sources3
Beta strandi334 – 340Combined sources7
Helixi341 – 351Combined sources11
Helixi355 – 358Combined sources4
Helixi361 – 370Combined sources10
Beta strandi373 – 380Combined sources8
Turni383 – 387Combined sources5
Helixi388 – 391Combined sources4
Beta strandi408 – 410Combined sources3
Turni412 – 415Combined sources4
Helixi417 – 423Combined sources7
Beta strandi428 – 438Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y9NX-ray2.89A19-449[»]
2YOKX-ray1.67A19-443[»]
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 – 449CatalyticAdd BLAST432
Regioni450 – 469LinkerAdd BLAST20

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF223252 Genomic DNA. Translation: AAF36391.1.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Y9NX-ray2.89A19-449[»]
2YOKX-ray1.67A19-443[»]
ProteinModelPortaliQ9P8P3.
SMRiQ9P8P3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.

Proteomic databases

PRIDEiQ9P8P3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 71 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

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.