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Protein

Exoglucanase 1

Gene

CBH1

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17639.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_PHACH.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Exoglucanase I
Gene namesi
Name:CBH1
OrganismiPhanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Taxonomic identifieri5306 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesPolyporalesPhanerochaetaceaePhanerochaete

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000792419 – 516Exoglucanase 1Add BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Glycosylationi442N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi488 ↔ 505By similarity
Disulfide bondi499 ↔ 515By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP13860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini480 – 516CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni? – 449Catalytic
Regioni450 – 480LinkerAdd BLAST31

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.

P13860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRTATLLAF TMAAMVFGQQ VGTNTARSHP ALTSQKCTKS GGCSNLNTKI
60 70 80 90 100
VLDANWRWLH STSGYTNCYT GNQWDATLCP DGKTCAANCA LDGADYTGTY
110 120 130 140 150
GITASGSSLK LQFVTGSNVG SRVYLMADDT HYQMFQLLNQ EFTFDVDMSN
160 170 180 190 200
LPCGLNGALY LSAMDADGGM AKYPTNKAGA KYGTGYCDSQ CPRDIKFING
210 220 230 240 250
EANVEGWNAT SANAGTGNYG TCCTEMDIWE ANNDAAAYTP HPCTTNAQTR
260 270 280 290 300
CSGSDCTRDT GLCDADGCDF NSFRMGDQTF LGKGLTVDTS KPFTVVTQFI
310 320 330 340 350
TNDGTSAGTL TEIRRLYVQN GKVIQNSSVK IPGIDPVNSI TDNFCSQQKT
360 370 380 390 400
AFGDTNYFAQ HGGLKQVGEA LRTGMVLALS IWDDYAANML WLDSNYPTNK
410 420 430 440 450
DPSTPGVARG TCATTSGVPA QIEAQSPNAY VVFSNIKFGD LNTTYTGTVS
460 470 480 490 500
SSSVSSSHSS TSTSSSHSSS STPPTQPTGV TVPQWGQCGG IGYTGSTTCA
510
SPYTCHVLNP YYSQCY
Length:516
Mass (Da):54,858
Last modified:January 1, 1990 - v1
Checksum:i1C7C3D338ECE1B72
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27 – 28RS → EN (PubMed:3246351).Curated2
Sequence conflicti30 – 31PA → RT (PubMed:3246351).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22220 Genomic DNA. Translation: AAB46373.1.
Z22528 mRNA. Translation: CAA80253.1.
PIRiJS0083.
S33164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22220 Genomic DNA. Translation: AAB46373.1.
Z22528 mRNA. Translation: CAA80253.1.
PIRiJS0083.
S33164.

3D structure databases

ProteinModelPortaliP13860.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_PHACH.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IE3Y. Eukaryota.
ENOG41101KD. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17639.

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_PHACH
AccessioniPrimary (citable) accession number: P13860
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. 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.