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B8MZ41 (AGDC_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. 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:AFLA_083300
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length877 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 – 877863Probable alpha/beta-glucosidase agdC
PRO_0000394915

Sites

Active site4221Nucleophile By similarity
Active site4251 By similarity
Active site5731Proton donor By similarity

Amino acid modifications

Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation6101N-linked (GlcNAc...) Potential
Glycosylation7441N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B8MZ41 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 52E2A673B0FFB6CF

FASTA87798,792
        10         20         30         40         50         60 
MLGSLLLLAP LAGAAVIGSR ADTKQCPGYK ASNVQENDRS LTADLTLAGK PCNTYGTDLQ 

        70         80         90        100        110        120 
NLKLLVEYQT DERLHVKIYD AEERVYQVPE KVTPRVDSGD GSSKDSALKF EYEEEPFSFT 

       130        140        150        160        170        180 
VKRDDEVLFD SSAENLIFQS QYLKLRTWLP ENPYLYGLGE HTDPLRLSTT NYTRTFWNRD 

       190        200        210        220        230        240 
AYGTPANSNL YGTHPVYYDH RGESGTHGVF LLNSNGMDVF IDKTADGKQY LEYNALGGIF 

       250        260        270        280        290        300 
DFYFFTGSNP KEASIEYSKI VGLPAMQSYW TFGLHQCRYG YRDVYQVAEV VYNYTKAGIP 

       310        320        330        340        350        360 
LETMWTDIDY MDRRRVFSLD PDRFPLEKMR ELVGYLHDHD QHYIVMVDPA VSVSDNGAFN 

       370        380        390        400        410        420 
RGLEQDVFLK TQNGSLYKGA VWPGVTAYPD WFHPDIQDYW NSEFSTFFNA ETGVDIDGLW 

       430        440        450        460        470        480 
IDMNEASNFC PDPCTDPERY SSENNLPPAP PPVRSSSPRP LPGFPADFQP SSASRSQKRI 

       490        500        510        520        530        540 
VKAKVGLEGR DLLNPPYKIR NEAGSLSNKT INTGIVHAGE GYAEYDTHNL YGTMMSSSSR 

       550        560        570        580        590        600 
EAMQYRRPEV RPLVITRSTY AGAGRDVGHW LGDNFSKWEH YRISIAEGLA FASMFQVPMV 

       610        620        630        640        650        660 
GADVCGFAGN TTEELCARWA SLGAFFTFYR NHNEIGNIGQ EFYVWPTVAE SARKAIDIRY 

       670        680        690        700        710        720 
RLLDYIYTSF YKQSQTGEPF LQPVFYLYPE DENTFSIDLQ FFYGDAILVS PVPDKGLTSV 

       730        740        750        760        770        780 
DAYFPDDIFY DWYTGTPVRG HGANITLSNI DITHIPLHIR GGSIIPIRSS SAMTTTELRE 

       790        800        810        820        830        840 
KSFQLIIAPG LDGTASGSLY LDDGDSLEQK ATLEVEFEYR KGVLHIDGKF ELHASLVESV 

       850        860        870 
TLLGQGKGGS RARREDGTKK TIQTNLELSK PTEIKLE 

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References

[1]"Genome sequence of Aspergillus flavus strain NRRL 3357."
Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ963472 Genomic DNA. Translation: EED57633.1.
RefSeqXP_002373245.1. XM_002373204.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5059.CADAFLAP00001110.

Proteomic databases

PRIDEB8MZ41.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFLAT00001110; CADAFLAP00001110; CADAFLAG00001110.
GeneID7916327.
KEGGafv:AFLA_083300.

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000041175.
KOK01187.
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_ASPFN
AccessionPrimary (citable) accession number: B8MZ41
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 32 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