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Protein

Exoglucanase 1

Gene

cbh1

Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed-Annotation score: 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 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 sitei1431 Publication1
Active sitei229Nucleophile1 Publication1
Active sitei234Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16499.
BRENDAi3.2.1.176. 6451.
3.2.1.91. 6451.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_TRIRE.

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
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [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 – 17Add BLAST17
ChainiPRO_000000792718 – 513Exoglucanase 1Add BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Pyrrolidone carboxylic acid1
Disulfide bondi21 ↔ 89
Disulfide bondi36 ↔ 42
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi67 ↔ 88
Disulfide bondi78 ↔ 84
Glycosylationi81N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi155 ↔ 414
Disulfide bondi189 ↔ 227
Disulfide bondi193 ↔ 226
Disulfide bondi247 ↔ 273
Disulfide bondi255 ↔ 260
Disulfide bondi278 ↔ 348
Glycosylationi287N-linked (GlcNAc...)Sequence analysis1
Glycosylationi401N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi485 ↔ 502
Disulfide bondi496 ↔ 512

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

STRINGi51453.JGI123989.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Beta strandi30 – 36Combined sources7
Beta strandi42 – 51Combined sources10
Helixi53 – 55Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi66 – 69Combined sources4
Turni75 – 77Combined sources3
Helixi81 – 87Combined sources7
Beta strandi88 – 90Combined sources3
Helixi95 – 99Combined sources5
Beta strandi101 – 104Combined sources4
Beta strandi107 – 121Combined sources15
Beta strandi123 – 130Combined sources8
Beta strandi136 – 138Combined sources3
Beta strandi142 – 149Combined sources8
Beta strandi157 – 164Combined sources8
Turni168 – 174Combined sources7
Helixi182 – 184Combined sources3
Beta strandi198 – 200Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi222 – 226Combined sources5
Beta strandi229 – 235Combined sources7
Beta strandi240 – 245Combined sources6
Beta strandi247 – 249Combined sources3
Beta strandi253 – 256Combined sources4
Helixi257 – 260Combined sources4
Turni262 – 264Combined sources3
Beta strandi265 – 267Combined sources3
Beta strandi268 – 273Combined sources6
Turni282 – 286Combined sources5
Beta strandi290 – 294Combined sources5
Beta strandi297 – 300Combined sources4
Beta strandi305 – 311Combined sources7
Beta strandi317 – 323Combined sources7
Beta strandi326 – 329Combined sources4
Beta strandi333 – 335Combined sources3
Beta strandi338 – 343Combined sources6
Helixi345 – 355Combined sources11
Helixi359 – 362Combined sources4
Helixi365 – 374Combined sources10
Beta strandi375 – 385Combined sources11
Turni387 – 391Combined sources5
Helixi392 – 395Combined sources4
Beta strandi396 – 399Combined sources4
Beta strandi412 – 414Combined sources3
Helixi421 – 427Combined sources7
Beta strandi432 – 442Combined sources11
Turni479 – 482Combined sources4
Beta strandi483 – 489Combined sources7
Beta strandi498 – 500Combined sources3
Beta strandi502 – 506Combined sources5
Beta strandi509 – 512Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZ6NMR-A478-513[»]
1AZHNMR-A478-513[»]
1AZJNMR-A478-513[»]
1AZKNMR-A478-513[»]
1CBHNMR-A478-513[»]
1CELX-ray1.80A/B19-451[»]
1DY4X-ray1.90A19-451[»]
1EGNX-ray1.60A18-451[»]
1Q2BX-ray1.60A18-451[»]
1Q2EX-ray1.75A/B19-451[»]
2CBHNMR-A478-513[»]
2CELX-ray2.00A/B19-451[»]
2MWJNMR-A478-513[»]
2MWKNMR-A478-513[»]
2V3IX-ray1.05A19-451[»]
2V3RX-ray1.60A19-451[»]
3CELX-ray2.00A19-451[»]
4C4CX-ray1.45A19-451[»]
4C4DX-ray1.32A19-451[»]
4CELX-ray2.20A/B19-451[»]
4D5IX-ray1.42A19-451[»]
4D5JX-ray1.50A19-451[»]
4D5OX-ray1.52A19-451[»]
4D5PX-ray1.89A19-451[»]
4D5QX-ray1.68A19-451[»]
4D5VX-ray1.62A19-451[»]
4P1HX-ray1.50A19-449[»]
4P1JX-ray2.62A19-451[»]
4UWTX-ray1.20A19-451[»]
4V0ZX-ray1.70A19-451[»]
5CELX-ray1.90A19-451[»]
6CELX-ray1.70A19-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ProteinModelPortaliP62694.
SMRiP62694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62694.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini477 – 513CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 453CatalyticAdd BLAST436
Regioni454 – 477LinkerAdd BLAST24

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IE3Y. Eukaryota.
ENOG41101KD. LUCA.

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.

P62694-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV
60 70 80 90 100
IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG
110 120 130 140 150
VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV
160 170 180 190 200
SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI
210 220 230 240 250
NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV
260 270 280 290 300
GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
310 320 330 340 350
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA
360 370 380 390 400
EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT
410 420 430 440 450
NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS
460 470 480 490 500
GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT
510
TCQVLNPYYS QCL
Length:513
Mass (Da):54,073
Last modified:July 21, 1986 - v1
Checksum:i9F5C0A8A854F2C12
GO

Sequence databases

PIRiA00902. EUTQI.

Cross-referencesi

Sequence databases

PIRiA00902. EUTQI.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZ6NMR-A478-513[»]
1AZHNMR-A478-513[»]
1AZJNMR-A478-513[»]
1AZKNMR-A478-513[»]
1CBHNMR-A478-513[»]
1CELX-ray1.80A/B19-451[»]
1DY4X-ray1.90A19-451[»]
1EGNX-ray1.60A18-451[»]
1Q2BX-ray1.60A18-451[»]
1Q2EX-ray1.75A/B19-451[»]
2CBHNMR-A478-513[»]
2CELX-ray2.00A/B19-451[»]
2MWJNMR-A478-513[»]
2MWKNMR-A478-513[»]
2V3IX-ray1.05A19-451[»]
2V3RX-ray1.60A19-451[»]
3CELX-ray2.00A19-451[»]
4C4CX-ray1.45A19-451[»]
4C4DX-ray1.32A19-451[»]
4CELX-ray2.20A/B19-451[»]
4D5IX-ray1.42A19-451[»]
4D5JX-ray1.50A19-451[»]
4D5OX-ray1.52A19-451[»]
4D5PX-ray1.89A19-451[»]
4D5QX-ray1.68A19-451[»]
4D5VX-ray1.62A19-451[»]
4P1HX-ray1.50A19-449[»]
4P1JX-ray2.62A19-451[»]
4UWTX-ray1.20A19-451[»]
4V0ZX-ray1.70A19-451[»]
5CELX-ray1.90A19-451[»]
6CELX-ray1.70A19-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ProteinModelPortaliP62694.
SMRiP62694.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi51453.JGI123989.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_TRIRE.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IE3Y. Eukaryota.
ENOG41101KD. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16499.
BRENDAi3.2.1.176. 6451.
3.2.1.91. 6451.

Miscellaneous databases

EvolutionaryTraceiP62694.

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_HYPJE
AccessioniPrimary (citable) accession number: P62694
Secondary accession number(s): P00725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 30, 2016
This is version 83 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

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.