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Protein

Alpha/beta-glucosidase agdC

Gene

agdC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

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 sitei429 – 4291NucleophileBy similarity
Active sitei432 – 4321By similarity
Active sitei600 – 6001Proton donorBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: UniProtKB
  2. beta-glucosidase activity Source: UniProtKB
  3. carbohydrate binding Source: InterPro
  4. glucosidase activity Source: ASPGD
  5. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha/beta-glucosidase agdC (EC:3.2.1.20, EC:3.2.1.21)
Gene namesi
Name:agdC
Synonyms:agdD
ORF Names:AN7345
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome IV

Subcellular locationi

  1. 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 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 894873Alpha/beta-glucosidase agdCPRO_0000394919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi802 – 8021N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00000088.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000041175.
InParanoidiQ5AWI5.
KOiK01187.
OMAiHVPMVGA.
OrthoDBiEOG77T1CZ.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
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.

Sequencei

Sequence statusi: Complete.

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

Q5AWI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTLLSWTP LALALMARAL SQLPLTDCPG YRVINVEERP RGLTADLTLA
60 70 80 90 100
GTPCNVYGVD IENLRLETDY DTNQRLHVKI YDADENVYQV PDSVFPRPVV
110 120 130 140 150
NDQACADENT PELRFSYAED PFSFAVSRAS NDETLFNTTG HNLIFQSQYV
160 170 180 190 200
NLRTSLPQNP NLYGLGEHSD PLRLNTINYT RTLWNRDAYT IPAGTNLYGA
210 220 230 240 250
HPMYIDHRGE AGTHGVFLLN SNGMDIKIDK NSDNIQFLEY NILGGVLDFY
260 270 280 290 300
FFAGPSPKDV SVQYAEVAGL PAMVPYWGLG FHQCRYGYRD IFEVAAVVHN
310 320 330 340 350
YSEARIPLET MWTDIDYMDH RKVFTLDRER FPLDTVRALV QYLHQRDQHY
360 370 380 390 400
IVMVDPAVAH SENGAFTRGL EKDVFMRKQD GTLYQGAVWP GATVFPDWFH
410 420 430 440 450
PNTSDYWINE FALFFNAESG VDIDALWIDM NEAANFCDWP CTDPVAYAEE
460 470 480 490 500
NNLPPEPPAV RPNPSSLPGF PAEFQPVNSN NNNSSRKRET QVVIAARQGF
510 520 530 540 550
VKVGNDNGNG RRLGLQGREL IDPPYKIANA AGSLSNKTMN TDIFHANGLA
560 570 580 590 600
EYDTHNLYGT MMSSLSRDAM LYRRPEKRPL VITRSTFAGA GSYVGHWLGD
610 620 630 640 650
NASTWTKYRI SIAQMLAFAS IFQIPMVGSD ACGFTGNTTE ELCSRWATLA
660 670 680 690 700
AFNPFFRNHN EYGMVSQEFY RWNSVAEAAR KAISIRYSLL DYLYTEFHEQ
710 720 730 740 750
TVTGEPFLLP LFFVYPNDPN VVGIDSQFFY GDAILVSPVI EEGKTEVHAY
760 770 780 790 800
FPGDLFYDWY TGLPLRGNGE VITLTDIGYT DIPLHVRGGK IVPVRTGSAG
810 820 830 840 850
MNTTTEVRKS GFRLVIAPGL DGRAAGRLYI DDGESLEQTA MVDVVFTYED
860 870 880 890
GRVSVDGVFT LQTDLRVEAV TVFGDNVVER TIDLPLSGPG GVEL
Length:894
Mass (Da):100,075
Last modified:June 15, 2010 - v2
Checksum:i6AE3AD13A10C594D
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490507 mRNA. Translation: ABF50883.1.
AACD01000128 Genomic DNA. Translation: EAA61716.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF78576.1.
RefSeqiXP_680614.1. XM_675522.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000088; CADANIAP00000088; CADANIAG00000088.
GeneIDi2869771.
KEGGiani:AN7345.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490507 mRNA. Translation: ABF50883.1.
AACD01000128 Genomic DNA. Translation: EAA61716.1. Sequence problems.
BN001304 Genomic DNA. Translation: CBF78576.1.
RefSeqiXP_680614.1. XM_675522.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00000088.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000088; CADANIAP00000088; CADANIAG00000088.
GeneIDi2869771.
KEGGiani:AN7345.2.

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000041175.
InParanoidiQ5AWI5.
KOiK01187.
OMAiHVPMVGA.
OrthoDBiEOG77T1CZ.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiAGDC_EMENI
AccessioniPrimary (citable) accession number: Q5AWI5
Secondary accession number(s): C8VCK6, Q1HFR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: April 1, 2015
This is version 58 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.