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Protein

1,4-beta-D-glucan cellobiohydrolase C

Gene

cbhC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: -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. Active against carboxymethylcellulose, beta-glucan and lichenan.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

pH dependencei

Optimum pH is 5.5.1 Publication

Temperature dependencei

Optimum temperature is 57 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei185PROSITE-ProRule annotation1
Active sitei231Proton donorPROSITE-ProRule annotation1
Active sitei410NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

  • cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB
  • cellulose binding Source: InterPro

GO - Biological processi

  • cellulose catabolic process Source: UniProtKB-KW
  • glucan catabolic process Source: UniProtKB

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM1 Carbohydrate-Binding Module Family 1
GH6 Glycoside Hydrolase Family 6
mycoCLAPiCBH6C_EMENI

Names & Taxonomyi

Protein namesi
Recommended name:
1,4-beta-D-glucan cellobiohydrolase C (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene namesi
Name:cbhC
ORF Names:AN5282
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome V
  • UP000005890 Componenti: Unassembled WGS sequence

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 – 19Sequence analysisAdd BLAST19
ChainiPRO_000039405320 – 4551,4-beta-D-glucan cellobiohydrolase CAdd BLAST436

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 44By similarity
Disulfide bondi38 ↔ 54By similarity
Disulfide bondi186 ↔ 245By similarity
Disulfide bondi377 ↔ 424By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ5B2E8

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003822

Structurei

3D structure databases

ProteinModelPortaliQ5B2E8
SMRiQ5B2E8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 55CBM1PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 92Thr-rich linkerAdd BLAST34
Regioni93 – 450CatalyticAdd BLAST358

Domaini

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000178851
InParanoidiQ5B2E8
KOiK19668
OrthoDBiEOG092C3X6S

Family and domain databases

Gene3Di3.20.20.40, 1 hit
InterProiView protein in InterPro
IPR016288 Beta_cellobiohydrolase
IPR036434 Beta_cellobiohydrolase_sf
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR001524 Glyco_hydro_6_CS
PANTHERiPTHR34876 PTHR34876, 1 hit
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF01341 Glyco_hydro_6, 1 hit
PIRSFiPIRSF001100 Beta_cellobiohydrolase, 1 hit
PRINTSiPR00733 GLHYDRLASE6
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821 CBD_fun, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF51989 SSF51989, 1 hit
SSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit
PS00655 GLYCOSYL_HYDROL_F6_1, 1 hit
PS00656 GLYCOSYL_HYDROL_F6_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5B2E8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHYSASGLAL AFLLPAIQAQ QTLYGQCGGS GWTGATSCVA GAACSTLNQW
60 70 80 90 100
YAQCLPAATT TSTTLTTTTS SVTTTSNPGS TTTTSSVTVT ATASGNPFSG
110 120 130 140 150
YQLYVNPYYS SEVQSIAIPS LTGTLSSLAP AATAAAKVPS FVWLDVAAKV
160 170 180 190 200
PTMATYLADI RSQNAAGANP PIAGQFVVYD LPDRDCAALA SNGEFAISDG
210 220 230 240 250
GVQHYKDYID SIREILVEYS DVHVILVIEP DSLANLVTNL NVAKCANAQS
260 270 280 290 300
AYLECTNYAV TQLNLPNVAM YLDAGHAGWL GWPANLQPAA NLYAGVYSDA
310 320 330 340 350
GSPAALRGLA TNVANYNAWA IDTCPSYTQG NSVCDEKDYI NALAPLLRAQ
360 370 380 390 400
GFDAHFITDT GRNGKQPTGQ QAWGDWCNVI GTGFGARPST NTGDSLLDAF
410 420 430 440 450
VWVKPGGESD GTSDTSAARY DAHCGYSDAL QPAPEAGTWF QAYFVQLLQN

ANPSF
Length:455
Mass (Da):47,624
Last modified:May 18, 2010 - v2
Checksum:i32C2655B3E4CCA1F
GO

Sequence cautioni

The sequence CBF82181 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAA62442 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490497 mRNA Translation: ABF50873.1
AACD01000093 Genomic DNA Translation: EAA62442.1 Sequence problems.
BN001305 Genomic DNA Translation: CBF82181.1 Sequence problems.
RefSeqiXP_662886.1, XM_657794.1

Genome annotation databases

EnsemblFungiiEAA62442; EAA62442; AN5282.2
GeneIDi2871574
KEGGiani:AN5282.2

Similar proteinsi

Entry informationi

Entry nameiCBHC_EMENI
AccessioniPrimary (citable) accession number: Q5B2E8
Secondary accession number(s): C8VH03, Q1HFS7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: June 20, 2018
This is version 71 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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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