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Q5B2E8

- CBHC_EMENI

UniProt

Q5B2E8 - CBHC_EMENI

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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: 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. 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851PROSITE-ProRule annotation
Active sitei231 – 2311Proton donorPROSITE-ProRule annotation
Active sitei410 – 4101NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. glucan catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

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
ProteomesiUP000000560: Chromosome V

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 4554361,4-beta-D-glucan cellobiohydrolase CPRO_0000394053Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 44By similarity
Disulfide bondi38 ↔ 54By similarity
Disulfide bondi186 ↔ 245By similarity
Disulfide bondi377 ↔ 424By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00003822.

Structurei

3D structure databases

ProteinModelPortaliQ5B2E8.
SMRiQ5B2E8. Positions 21-55, 90-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5536CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 9234Thr-rich linkerAdd
BLAST
Regioni93 – 450358CatalyticAdd
BLAST

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

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5297.
HOGENOMiHOG000178851.
InParanoidiQ5B2E8.
OrthoDBiEOG72C594.

Family and domain databases

Gene3Di3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFiPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSiPR00733. GLHYDRLASE6.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

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 CBF82181.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence EAA62442.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsemblFungiiCADANIAT00003822; CADANIAP00003822; CADANIAG00003822.
GeneIDi2871574.
KEGGiani:AN5282.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ490497 mRNA. Translation: ABF50873.1 .
AACD01000093 Genomic DNA. Translation: EAA62442.1 . Sequence problems.
BN001305 Genomic DNA. Translation: CBF82181.1 . Sequence problems.
RefSeqi XP_662886.1. XM_657794.1.

3D structure databases

ProteinModelPortali Q5B2E8.
SMRi Q5B2E8. Positions 21-55, 90-455.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00003822.

Protein family/group databases

mycoCLAPi CBH6C_EMENI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00003822 ; CADANIAP00003822 ; CADANIAG00003822 .
GeneIDi 2871574.
KEGGi ani:AN5282.2.

Phylogenomic databases

eggNOGi COG5297.
HOGENOMi HOG000178851.
InParanoidi Q5B2E8.
OrthoDBi EOG72C594.

Family and domain databases

Gene3Di 3.20.20.40. 1 hit.
InterProi IPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view ]
PIRSFi PIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSi PR00733. GLHYDRLASE6.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiCBHC_EMENI
AccessioniPrimary (citable) accession number: Q5B2E8
Secondary accession number(s): C8VH03, Q1HFS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 54 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

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

External Data

Dasty 3