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Q0CMA7 (AGDC_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:
Probable alpha/beta-glucosidase agdC

EC=3.2.1.20
EC=3.2.1.21
Gene names
Name:agdC
ORF Names:ATEG_05177
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

maltose alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 879865Probable alpha/beta-glucosidase agdC
PRO_0000394918

Sites

Active site4261Nucleophile By similarity
Active site4291 By similarity
Active site5801Proton donor By similarity

Amino acid modifications

Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Potential
Glycosylation6171N-linked (GlcNAc...) Potential
Glycosylation7871N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q0CMA7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 7D0D7DA1D2763950

FASTA87998,442
        10         20         30         40         50         60 
MLGSLLLLAP LAGAAVIGSR SNNTEPCPGY KVSNVREGVN SLTADLSLAG KPCNTYGTDL 

        70         80         90        100        110        120 
KDLKLLVEYQ TERPDERLHV MIYDANEQVY QVPESVVPRV EGRKGARPHS ALKFTYEEEP 

       130        140        150        160        170        180 
FSFTVTRDDE VLFDTSASNL IFQSQYLNLR TWLPEDPYLY GLGEHTDSLR LPTTNYTRTI 

       190        200        210        220        230        240 
WNRDSYGVPQ NSNLYGAHPV YYDHRGESGT HGVFLLNSNG MDIRIDKTED GQQYLEYNTL 

       250        260        270        280        290        300 
GGVFDFYFFT GSTPKETSME YSKIVGLPAM QSYWSFGLHQ CRYGYRDVYQ VAEVVYNYSK 

       310        320        330        340        350        360 
AGIPLETMWT DIDYMNARKV FTLDPERFPL PKMRELVDYL HKHDQKYIVM VDPAVSAVDN 

       370        380        390        400        410        420 
EAYEHGVDQG IFLQQQNGSL YKGAVWPGVT VYPDWFHPDI QEYWNSEFSA FFSADDGVDI 

       430        440        450        460        470        480 
DGLWIDMNEA ANFCTWPCAD PEQYAIDNDL PPAPPAVRPS NPRPLPGFPD SFQPSSSKRA 

       490        500        510        520        530        540 
VKRAGGSKGA KVGLPGRNLV DPPYKIQNAA GSISNKTINT DIIHAGEGYA EYDTHNLYGT 

       550        560        570        580        590        600 
MMSSASRGAM LNRRPDVRPL IITRSTFAGA GSHVGHWLGD NLSQWDQYRI SISQIVAFAS 

       610        620        630        640        650        660 
MFQVPMVGAD VCGFGGNTTE ELCARWAALG AFYTFYRNHN EIGSTSQEFY QWPTVADSAR 

       670        680        690        700        710        720 
KAIEIRYKLL DYIYTAFHKQ TETGEPFLQP MFYLYPEDEN TFANDVQFFY GDALLVSPVL 

       730        740        750        760        770        780 
TEGSTSVDAY FPDDIFYDWY TGAPVRGHGA KKTLENIDVT HIPLHVRGGN IIPVRSSGAM 

       790        800        810        820        830        840 
TTKELRNKSF ELIIAPGLDG TASGSLYLDD GDSLEQKGTA EIKFEYRRGK LSVKGSFGRS 

       850        860        870 
AAGVKVQAVK VLGQKAESRM SAFRSTEFEL TRPMEISLQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476600 Genomic DNA. Translation: EAU34246.1.
RefSeqXP_001214355.1. XM_001214355.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00004842.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00004842; CADATEAP00004842; CADATEAG00004842.
GeneID4320812.

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000041175.
OMASGQYLEY.
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.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAGDC_ASPTN
AccessionPrimary (citable) accession number: Q0CMA7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 36 of the entry and version 1 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