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Protein

Probable alpha/beta-glucosidase agdC

Gene

agdC

Organism
Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei422 – 4221NucleophilePROSITE-ProRule annotation
Active sitei425 – 4251By similarity
Active sitei571 – 5711Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable alpha/beta-glucosidase agdC (EC:3.2.1.20, EC:3.2.1.21)
Gene namesi
Name:agdC
ORF Names:AFUB_015590
OrganismiNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus)
Taxonomic identifieri451804 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001699 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1414Sequence AnalysisAdd
BLAST
Chaini15 – 881867Probable alpha/beta-glucosidase agdCPRO_0000394914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi742 – 7421N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000041175.
OrthoDBiEOG77T1CZ.
PhylomeDBiB0XNL6.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B0XNL6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSLLLLAP LVGAAVIGAR DHSQECPGYK ATNIREGRDS LTADLTLAGK
60 70 80 90 100
PCNTYGTDLK NLKLLVEYQT DKRLHVKIYD ADEEVYQVPE SVLPRVDGKG
110 120 130 140 150
GSSKKSALKF DYQANPFSFK VKRGGEVLFD TSGSNLIFQS QYLSLRTWLP
160 170 180 190 200
EDPNLYGLGE HTDSLRLETT NYTRTLWNRD AYAIPEKTNL YGTHPVYYDH
210 220 230 240 250
RGQHGTHGVF LLNSNGMDIK IDKTKDGKQY LEYNTLGGVF DFYFFTGATP
260 270 280 290 300
KDASIEYAKV VGLPAMQSYW TFGFHQCRYG YRDVFEVAEV VYNYSQAKIP
310 320 330 340 350
LETMWTDIDY MDRRRVFTLD PERFPLEKMR ELVSYLHNHN QHYIVMVDPA
360 370 380 390 400
VSVSDNVGYN DGMEQGIFLQ TQNGSLYKGA VWPGVTAYPD WFHPDIQKYW
410 420 430 440 450
NDQFAKFFDP KTGVDIDGLW IDMNEAANFC PYPCSDPEGY ARDNDLPPAA
460 470 480 490 500
PPVRPSNPRP LPGFPGDFQP SSSSKRSTKG SKVGLPNRDL INPPYMIRNE
510 520 530 540 550
AGSLSNKTIN TDIIHAGEGY AEYDTHNLYG TMMSSASRNA MQHRRPGVRP
560 570 580 590 600
LVITRSTYAG AGAHVGHWLG DNISEWSKYR ISISQMLAFA SMFQVPMIGS
610 620 630 640 650
DVCGFGGNTT EELCARWARL GAFYTFFRNH NEITGIPQEF YRWPTVAESA
660 670 680 690 700
RKAIDIRYRL LDYIYTAFHR QTQTGEPFLQ PMFYLYPKDK NTFSNQLQFF
710 720 730 740 750
YGDAILVSPV TDGSQTSVDA YFPDDIFYDW HTGAALRGRG ANVTLSNIDV
760 770 780 790 800
TEIPIHIRGG SIIPVRSESA MTTTELRKKG FELIIAPGLD GTASGSLYLD
810 820 830 840 850
DGDSIEPRAT LELEFTYRKG HLQVKGKFGF RTEVKINAVT LLGQSAPASK
860 870 880
SADVASLDSG RQAVTIKTSL DLTGPSEIDL S
Length:881
Mass (Da):98,888
Last modified:April 8, 2008 - v1
Checksum:i15EE1FAA6A1FDAD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499594 Genomic DNA. Translation: EDP56838.1.

Genome annotation databases

EnsemblFungiiCADAFUBT00001564; CADAFUBP00001528; CADAFUBG00001564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS499594 Genomic DNA. Translation: EDP56838.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUBT00001564; CADAFUBP00001528; CADAFUBG00001564.

Phylogenomic databases

HOGENOMiHOG000041175.
OrthoDBiEOG77T1CZ.
PhylomeDBiB0XNL6.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CEA10 / CBS 144.89 / FGSC A1163.

Entry informationi

Entry nameiAGDC_ASPFC
AccessioniPrimary (citable) accession number: B0XNL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 8, 2008
Last modified: April 1, 2015
This is version 32 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

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.