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Protein

Exoglucanase 1

Gene

cbh1

Organism
Trichoderma harzianum (Hypocrea lixii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (PubMed:21876370). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).Curated1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.2 Publications

Kineticsi

kcat is 23.2 min(-1) with p-nitrophenyl-D-cellobioside as substrate and 44.6 min(-1) with 2-chloro-4-nitrophenyl-beta-lactoside as substrate.1 Publication
  1. KM=3.4 mM for p-nitrophenyl-D-cellobioside1 Publication
  2. KM=3.7 mM for 2-chloro-4-nitrophenyl-beta-lactoside1 Publication
  1. Vmax=0.016 mmol/min/mg enzyme for p-nitrophenyl-D-cellobioside1 Publication
  2. Vmax=0.031 mmol/min/mg enzyme for 2-chloro-4-nitrophenyl-beta-lactoside1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Temperature dependencei

Optimum temperature is 50 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei225Nucleophile1 Publication1
Active sitei230Proton donor/acceptor1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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
Cellobiohydrolase 7A
Short name:
Cel7A
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiTrichoderma harzianum (Hypocrea lixii)
Taxonomic identifieri5544 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 acid1 Publication1
Disulfide bondi21 ↔ 881 Publication
Disulfide bondi36 ↔ 411 Publication
Disulfide bondi66 ↔ 871 Publication
Disulfide bondi77 ↔ 831 Publication
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi151 ↔ 4101 Publication
Disulfide bondi185 ↔ 2231 Publication
Disulfide bondi189 ↔ 2221 Publication
Disulfide bondi243 ↔ 2691 Publication
Disulfide bondi251 ↔ 2561 Publication
Disulfide bondi274 ↔ 3441 Publication
Glycosylationi283N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi397N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

O-glycosylated. O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose.By 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 – 449Catalytic1 PublicationAdd BLAST432
Regioni450 – 468LinkerCuratedAdd BLAST19

Domaini

The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiView protein in InterPro
IPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
PfamiView protein in Pfam
PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
PRINTSiPR00734. GLHYDRLASE7.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821. CBD_fun. 1 hit.
SMARTiView protein in SMART
SM00236. fCBD. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiView protein in PROSITE
PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiGUX1_TRIHA
AccessioniPrimary (citable) accession number: Q9P8P3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: August 30, 2017
This is version 74 of the entry and version 1 of the sequence. See 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