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Protein

Exoglucanase 1

Gene

CBH-1

Organism
Humicola grisea var. thermoidea
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 sitei231NucleophileBy similarity1
Active sitei236Proton 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
Beta-glucancellobiohydrolase
Exocellobiohydrolase I
Exoglucanase I
Gene namesi
Name:CBH-1
OrganismiHumicola grisea var. thermoidea
Taxonomic identifieri5528 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeHumicola

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000792119 – 525Exoglucanase 1Add BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi289N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi497 ↔ 514By similarity
Disulfide bondi508 ↔ 524By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP15828.

Structurei

Secondary structure

1525
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 38Combined sources8
Turni39 – 41Combined sources3
Beta strandi42 – 52Combined sources11
Helixi54 – 56Combined sources3
Beta strandi59 – 65Combined sources7
Beta strandi67 – 70Combined sources4
Turni76 – 78Combined sources3
Helixi82 – 88Combined sources7
Beta strandi89 – 91Combined sources3
Helixi96 – 100Combined sources5
Beta strandi102 – 105Combined sources4
Beta strandi108 – 116Combined sources9
Beta strandi121 – 123Combined sources3
Beta strandi125 – 136Combined sources12
Beta strandi144 – 151Combined sources8
Beta strandi159 – 166Combined sources8
Turni170 – 176Combined sources7
Helixi184 – 186Combined sources3
Beta strandi200 – 202Combined sources3
Beta strandi224 – 228Combined sources5
Beta strandi231 – 237Combined sources7
Beta strandi242 – 247Combined sources6
Beta strandi249 – 251Combined sources3
Beta strandi255 – 258Combined sources4
Helixi259 – 262Combined sources4
Beta strandi265 – 267Combined sources3
Turni268 – 271Combined sources4
Beta strandi273 – 275Combined sources3
Turni284 – 288Combined sources5
Beta strandi292 – 294Combined sources3
Beta strandi297 – 300Combined sources4
Beta strandi305 – 313Combined sources9
Beta strandi317 – 328Combined sources12
Beta strandi331 – 334Combined sources4
Beta strandi346 – 348Combined sources3
Helixi350 – 360Combined sources11
Helixi365 – 368Combined sources4
Helixi371 – 380Combined sources10
Beta strandi383 – 391Combined sources9
Turni393 – 397Combined sources5
Helixi398 – 401Combined sources4
Beta strandi402 – 405Combined sources4
Helixi406 – 408Combined sources3
Turni412 – 414Combined sources3
Helixi426 – 432Combined sources7
Beta strandi437 – 447Combined sources11
Beta strandi450 – 452Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CSIX-ray1.80A/B20-457[»]
ProteinModelPortaliP15828.
SMRiP15828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini489 – 525CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 467CatalyticAdd BLAST449
Regioni468 – 489LinkerAdd BLAST22

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.

P15828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTAKFATLA ALVASAAAQQ ACSLTTERHP SLSWNKCTAG GQCQTVQASI
60 70 80 90 100
TLDSNWRWTH QVSGSTNCYT GNKWDTSICT DAKSCAQNCC VDGADYTSTY
110 120 130 140 150
GITTNGDSLS LKFVTKGQHS TNVGSRTYLM DGEDKYQTFE LLGNEFTFDV
160 170 180 190 200
DVSNIGCGLN GALYFVSMDA DGGLSRYPGN KAGAKYGTGY CDAQCPRDIK
210 220 230 240 250
FINGEANIEG WTGSTNDPNA GAGRYGTCCS EMDIWEANNM ATAFTPHPCT
260 270 280 290 300
IIGQSRCEGD SCGGTYSNER YAGVCDPDGC DFNSYRQGNK TFYGKGMTVD
310 320 330 340 350
TTKKITVVTQ FLKDANGDLG EIKRFYVQDG KIIPNSESTI PGVEGNSITQ
360 370 380 390 400
DWCDRQKVAF GDIDDFNRKG GMKQMGKALA GPMVLVMSIW DDHASNMLWL
410 420 430 440 450
DSTFPVDAAG KPGAERGACP TTSGVPAEVE AEAPNSNVVF SNIRFGPIGS
460 470 480 490 500
TVAGLPGAGN GGNNGGNPPP PTTTTSSAPA TTTTASAGPK AGRWQQCGGI
510 520
GFTGPTQCEE PYICTKLNDW YSQCL
Length:525
Mass (Da):55,694
Last modified:February 1, 1996 - v2
Checksum:iA6684D4CF881E090
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17258 Genomic DNA. Translation: CAA35159.1.
PIRiS38794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17258 Genomic DNA. Translation: CAA35159.1.
PIRiS38794.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CSIX-ray1.80A/B20-457[»]
ProteinModelPortaliP15828.
SMRiP15828.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

Proteomic databases

PRIDEiP15828.

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_HUMGT
AccessioniPrimary (citable) accession number: P15828
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 97 of the entry and version 2 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.