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Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

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-Protein inferred from homologyi

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).By similarity

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981Proton donorBy similarity
Active sitei296 – 2961NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 1
Exo-1,3-beta-glucanase A
Gene namesi
Name:exgA
Synonyms:exg1
ORF Names:AN4052
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome II

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 405379Probable glucan 1,3-beta-glucosidase APRO_0000393532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi278 ↔ 403By similarity
Disulfide bondi304 ↔ 330By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi162425.CADANIAP00004629.

Structurei

3D structure databases

ProteinModelPortaliQ5B5X8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ5B5X8.
KOiK01210.
OrthoDBiEOG7JT75H.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5B5X8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPRISQAAI LAHSLLAVCT SAATLAEKVR GVNLGGWLVL EPWITPSLFD
60 70 80 90 100
EAGDEAVDEY TLTEVLGVEE AAARLSEHWN TFITEEDFAL IAEAGLNYVR
110 120 130 140 150
IPIGYWAAAP LDGEPYVSGQ LEHLDNAVAW ARAHNLKVIV DLHGAPGSQN
160 170 180 190 200
GFDNSGRRGP IGWQQGDTVE QTILAFETLA QRYLADDDTV TMIEALNEPH
210 220 230 240 250
VPGGINQDQL KDYYEETLAR VRKNSPEATL LLHDGFVQTE GWNGFMTGEN
260 270 280 290 300
VMMDTHHYEV FEGGQNAWSI EKHIDAACQL GRQHLQAADK PVIVGEWTGA
310 320 330 340 350
LSDCTRYLNG KGIGIRYDGT LGSNTAVGAC GSKSEGSVAG LSADEIANTR
360 370 380 390 400
RFIEAQLDAF ELRNGWVFWT WKTEGAPGWD MQDLLANGVF PQPLTDREFP

NQCNF
Length:405
Mass (Da):44,437
Last modified:April 19, 2010 - v2
Checksum:iDBC5551A2C1E64B8
GO

Sequence cautioni

The sequence CBF74803.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA59523.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000065 Genomic DNA. Translation: EAA59523.1. Sequence problems.
BN001302 Genomic DNA. Translation: CBF74803.1. Sequence problems.
RefSeqiXP_661656.1. XM_656564.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004629; CADANIAP00004629; CADANIAG00004629.
GeneIDi2873465.
KEGGiani:AN4052.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACD01000065 Genomic DNA. Translation: EAA59523.1. Sequence problems.
BN001302 Genomic DNA. Translation: CBF74803.1. Sequence problems.
RefSeqiXP_661656.1. XM_656564.1.

3D structure databases

ProteinModelPortaliQ5B5X8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00004629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00004629; CADANIAP00004629; CADANIAG00004629.
GeneIDi2873465.
KEGGiani:AN4052.2.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ5B5X8.
KOiK01210.
OrthoDBiEOG7JT75H.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiEXGA_EMENI
AccessioniPrimary (citable) accession number: Q5B5X8
Secondary accession number(s): C8V5I6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 19, 2010
Last sequence update: April 19, 2010
Last modified: January 6, 2015
This is version 65 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

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.