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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 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 sitei231 – 2311NucleophileBy similarity
Active sitei236 – 2361Proton donorBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 525507Exoglucanase 1PRO_0000007921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi497 ↔ 514By similarity
Disulfide bondi508 ↔ 524By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP15828.

Structurei

Secondary structure

1
525
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 388Combined sources
Turni39 – 413Combined sources
Beta strandi42 – 5211Combined sources
Helixi54 – 563Combined sources
Beta strandi59 – 657Combined sources
Beta strandi67 – 704Combined sources
Turni76 – 783Combined sources
Helixi82 – 887Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 1005Combined sources
Beta strandi102 – 1054Combined sources
Beta strandi108 – 1169Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi125 – 13612Combined sources
Beta strandi144 – 1518Combined sources
Beta strandi159 – 1668Combined sources
Turni170 – 1767Combined sources
Helixi184 – 1863Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi224 – 2285Combined sources
Beta strandi231 – 2377Combined sources
Beta strandi242 – 2476Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi255 – 2584Combined sources
Helixi259 – 2624Combined sources
Beta strandi265 – 2673Combined sources
Turni268 – 2714Combined sources
Beta strandi273 – 2753Combined sources
Turni284 – 2885Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi297 – 3004Combined sources
Beta strandi305 – 3139Combined sources
Beta strandi317 – 32812Combined sources
Beta strandi331 – 3344Combined sources
Beta strandi346 – 3483Combined sources
Helixi350 – 36011Combined sources
Helixi365 – 3684Combined sources
Helixi371 – 38010Combined sources
Beta strandi383 – 3919Combined sources
Turni393 – 3975Combined sources
Helixi398 – 4014Combined sources
Beta strandi402 – 4054Combined sources
Helixi406 – 4083Combined sources
Turni412 – 4143Combined sources
Helixi426 – 4327Combined sources
Beta strandi437 – 44711Combined sources
Beta strandi450 – 4523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CSIX-ray1.80A/B20-457[»]
ProteinModelPortaliP15828.
SMRiP15828. Positions 19-451, 491-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 52537CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 467449CatalyticAdd
BLAST
Regioni468 – 48922LinkerAdd
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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4CSIX-ray1.80A/B20-457[»]
ProteinModelPortaliP15828.
SMRiP15828. Positions 19-451, 491-525.
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

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...

Publicationsi

  1. "Sequence of cbh-1 gene of Humicola grisea var. thermoidea."
    de Oliviera Alzevedo M., Radford A.
    Nucleic Acids Res. 18:668-668(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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: February 4, 2015
This is version 91 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

External Data

Dasty 3

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 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.