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Protein

Probable 1,4-beta-D-glucan cellobiohydrolase A

Gene

cbhA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 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 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.By similarity

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 sitei226 – 2261NucleophileBy similarity
Active sitei231 – 2311Proton 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

CAZyiGH7. Glycoside Hydrolase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase A (EC:3.2.1.91)
Alternative name(s):
Beta-glucancellobiohydrolase A
Cellobiohydrolase D
Exocellobiohydrolase A
Exoglucanase A
Gene namesi
Name:cbhA
Synonyms:celD
ORF Names:AN5176
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome V

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 446429Probable 1,4-beta-D-glucan cellobiohydrolase APRO_0000393544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi284 – 2841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Repressed by D-glucose.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ5B2Q4.
SMRiQ5B2Q4. Positions 18-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
InParanoidiQ5B2Q4.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5B2Q4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYQRALLFSA LLSVSRAQQA GTAQEEVHPS LTWQRCEASG SCTEVAGSVV
60 70 80 90 100
LDSNWRWTHS VDGYTNCYTG NEWDATLCPD NESCAQNCAV DGADYEATYG
110 120 130 140 150
ITSNGDSLTL KFVTGSNVGS RVYLMEDDET YQMFDLLNNE FTFDVDVSNL
160 170 180 190 200
PCGLNGALYF TSMDADGGLS KYEGNTAGAK YGTGYCDSQC PRDIKFINGL
210 220 230 240 250
GNVEGWEPSD SDANAGVGGM GTCCPEMDIW EANSISTAYT PHPCDSVEQT
260 270 280 290 300
MCEGDSCGGT YSDDRYGGTC DPDGCDFNSY RMGNTSFYGP GAIIDTSSKF
310 320 330 340 350
TVVTQFIADG GSLSEIKRFY VQNGEVIPNS ESNISGVEGN SITSEFCTAQ
360 370 380 390 400
KTAFGDEDIF AQHGGLSAMG DAASAMVLIL SIWDDHHSSM MWLDSSYPTD
410 420 430 440
ADPSQPGVAR GTCEQGAGDP DVVESEHADA SVTFSNIKFG PIGSTF
Length:446
Mass (Da):47,638
Last modified:April 26, 2005 - v1
Checksum:iDACEE446E809A6D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501L → F in AAM54069 (PubMed:12409103).Curated
Sequence conflicti286 – 2861S → R in AAM54069 (PubMed:12409103).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420019 Genomic DNA. Translation: AAM54069.1.
DQ490495 mRNA. Translation: ABF50871.1.
AACD01000089 Genomic DNA. Translation: EAA62357.1.
BN001305 Genomic DNA. Translation: CBF81021.1.
RefSeqiXP_662780.1. XM_657688.1.

Genome annotation databases

EnsemblFungiiCADANIAT00003171; CADANIAP00003171; CADANIAG00003171.
GeneIDi2871468.
KEGGiani:AN5176.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF420019 Genomic DNA. Translation: AAM54069.1.
DQ490495 mRNA. Translation: ABF50871.1.
AACD01000089 Genomic DNA. Translation: EAA62357.1.
BN001305 Genomic DNA. Translation: CBF81021.1.
RefSeqiXP_662780.1. XM_657688.1.

3D structure databases

ProteinModelPortaliQ5B2Q4.
SMRiQ5B2Q4. Positions 18-446.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH7. Glycoside Hydrolase Family 7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00003171; CADANIAP00003171; CADANIAG00003171.
GeneIDi2871468.
KEGGiani:AN5176.2.

Phylogenomic databases

eggNOGiNOG85664.
HOGENOMiHOG000182210.
InParanoidiQ5B2Q4.
OMAiNWSKCTS.
OrthoDBiEOG7ZGXCF.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans."
    Lockington R.A., Rodbourn L., Barnett S., Carter C.J., Kelly J.M.
    Fungal Genet. Biol. 37:190-196(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "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 nameiCBHA_EMENI
AccessioniPrimary (citable) accession number: Q5B2Q4
Secondary accession number(s): C8VF49, Q1HFS9, Q8NK03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: April 26, 2005
Last modified: July 22, 2015
This is version 67 of the entry and version 1 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

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.