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Q5AWI5 (AGDC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha/beta-glucosidase agdC

EC=3.2.1.20
EC=3.2.1.21
Gene names
Name:agdC
Synonyms:agdD
ORF Names:AN7345
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length894 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity. Ref.1

Catalytic activity

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Sequence caution

The sequence EAA61716.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 894873Alpha/beta-glucosidase agdC
PRO_0000394919

Sites

Active site4291Nucleophile By similarity
Active site4321 By similarity
Active site6001Proton donor By similarity

Amino acid modifications

Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation6371N-linked (GlcNAc...) Potential
Glycosylation8021N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5AWI5 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 6AE3AD13A10C594D

FASTA894100,075
        10         20         30         40         50         60 
MAGTLLSWTP LALALMARAL SQLPLTDCPG YRVINVEERP RGLTADLTLA GTPCNVYGVD 

        70         80         90        100        110        120 
IENLRLETDY DTNQRLHVKI YDADENVYQV PDSVFPRPVV NDQACADENT PELRFSYAED 

       130        140        150        160        170        180 
PFSFAVSRAS NDETLFNTTG HNLIFQSQYV NLRTSLPQNP NLYGLGEHSD PLRLNTINYT 

       190        200        210        220        230        240 
RTLWNRDAYT IPAGTNLYGA HPMYIDHRGE AGTHGVFLLN SNGMDIKIDK NSDNIQFLEY 

       250        260        270        280        290        300 
NILGGVLDFY FFAGPSPKDV SVQYAEVAGL PAMVPYWGLG FHQCRYGYRD IFEVAAVVHN 

       310        320        330        340        350        360 
YSEARIPLET MWTDIDYMDH RKVFTLDRER FPLDTVRALV QYLHQRDQHY IVMVDPAVAH 

       370        380        390        400        410        420 
SENGAFTRGL EKDVFMRKQD GTLYQGAVWP GATVFPDWFH PNTSDYWINE FALFFNAESG 

       430        440        450        460        470        480 
VDIDALWIDM NEAANFCDWP CTDPVAYAEE NNLPPEPPAV RPNPSSLPGF PAEFQPVNSN 

       490        500        510        520        530        540 
NNNSSRKRET QVVIAARQGF VKVGNDNGNG RRLGLQGREL IDPPYKIANA AGSLSNKTMN 

       550        560        570        580        590        600 
TDIFHANGLA EYDTHNLYGT MMSSLSRDAM LYRRPEKRPL VITRSTFAGA GSYVGHWLGD 

       610        620        630        640        650        660 
NASTWTKYRI SIAQMLAFAS IFQIPMVGSD ACGFTGNTTE ELCSRWATLA AFNPFFRNHN 

       670        680        690        700        710        720 
EYGMVSQEFY RWNSVAEAAR KAISIRYSLL DYLYTEFHEQ TVTGEPFLLP LFFVYPNDPN 

       730        740        750        760        770        780 
VVGIDSQFFY GDAILVSPVI EEGKTEVHAY FPGDLFYDWY TGLPLRGNGE VITLTDIGYT 

       790        800        810        820        830        840 
DIPLHVRGGK IVPVRTGSAG MNTTTEVRKS GFRLVIAPGL DGRAAGRLYI DDGESLEQTA 

       850        860        870        880        890 
MVDVVFTYED GRVSVDGVFT LQTDLRVEAV TVFGDNVVER TIDLPLSGPG GVEL 

« Hide

References

« Hide 'large scale' references
[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.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ490507 mRNA. Translation: ABF50883.1.
AACD01000128 Genomic DNA. Translation: EAA61716.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF78576.1.
RefSeqXP_680614.1. XM_675522.1.

3D structure databases

ProteinModelPortalQ5AWI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00000088.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.
mycoCLAPAGL31C_EMENI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00000088; CADANIAP00000088; CADANIAG00000088.
GeneID2869771.
KEGGani:AN7345.2.

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000041175.
KOK01187.
OMAMMSTATH.
OrthoDBEOG77T1CZ.

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAGDC_EMENI
AccessionPrimary (citable) accession number: Q5AWI5
Secondary accession number(s): C8VCK6, Q1HFR7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 16, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries