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Protein

Exoglucanase 1

Gene

CBH1

Organism
Phanerochaete chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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

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 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000792419 – 516Exoglucanase 1Add BLAST498

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP13860

Structurei

3D structure databases

ProteinModelPortaliP13860
SMRiP13860
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

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
InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR013320 ConA-like_dom_sf
IPR001722 Glyco_hydro_7
IPR037019 Glyco_hydro_7_sf
PANTHERiPTHR33753 PTHR33753, 1 hit
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.

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

Similar proteinsi

Entry informationi

Entry nameiGUX1_PHACH
AccessioniPrimary (citable) accession number: P13860
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 105 of the entry and version 1 of the sequence. See 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

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