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Protein

Glucan 1,3-beta-glucosidase D

Gene

exgD

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. Active on lichenan.1 Publication

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei598 – 5981Proton donorBy similarity
Active sitei703 – 7031NucleophileBy 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

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5D_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase D (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase D
Gene namesi
Name:exgD
ORF Names:AN7533
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 300300CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei301 – 32121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini322 – 831510ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 831831Glucan 1,3-beta-glucosidase DPRO_0000395168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi547 – 5471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi611 – 6111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi637 – 6371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AVZ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 280275Arg-richAdd
BLAST
Compositional biasi33 – 7442Asp-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ5AVZ7.
KOiK01210.
OMAiNIITHYG.
OrthoDBiEOG7ZPNTV.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5AVZ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSQSRSRDR YGRDSDRDRS RVQPRRRYHV SEDDDDDDDF DDNPRDRRYR
60 70 80 90 100
RDGYRRAPVD SRAYDSHDDY EVVDVEEEPR RYRSDTERRR ERARASPGTS
110 120 130 140 150
PRKRERTRDS GGGHRRRRTE ESDGSQAPQA HRDRRSRTRR DRGLDDEDLE
160 170 180 190 200
DAARRLRRRE RERERERRAE TSKHKSTDSS NSSAGLLNAN ALAKLRAQHE
210 220 230 240 250
ELDRQEQRRA EKEAKAERKR RRKRPAVEGQ MRTLDPFPDE VPRGQSKGRI
260 270 280 290 300
VSGAYLEEGR APDMEVRLRG GGRGPPRERR WEKDSDGSAP LTPFWKRKKW
310 320 330 340 350
WWIGAIVLVI VVIIIVVAVV VSNNKKSDSD SDSDSNSGSS DSWGGDKSSL
360 370 380 390 400
NGLDHDSIPK SAQGTVLDPW TWYETTDFNV TYTDETVGGL SVMGLNSTWD
410 420 430 440 450
DSVAPNENVP PLNKPFPYGS QPIRGVNIGG LLSLEPFITP SLFEGYSSDV
460 470 480 490 500
VDEYTLTTKL GDNAARKLEE HYATFITEQD FADMAEAGID HVRIPFSYWA
510 520 530 540 550
VNPREDEPYV AKISWRYLLR VIEYCRKYGL RVNLDPHGMP GSQNGMNHSG
560 570 580 590 600
RQGSIRWLNG DDGDTYAQRS LEFHEKISKF FAQDRYKNII TIYGLINEPY
610 620 630 640 650
MLSLDVEKVL NWTVTAAELV QKNGITAKIA FHDGFLNLSK WKTMLKNGPS
660 670 680 690 700
NLLLDTHQYT IYNVAQIVLN HTAKVNFVCN DWVGMIGEIN STSEGWGPTI
710 720 730 740 750
CGEFTQADTD CAKNLNNVGR GTRWEGTYSE GDSTMYCPTA EQRTCSCTEA
760 770 780 790 800
NADPSEYSDD YKLFLKTYAE AQMYAFEQAQ GWFYWTWHTE SAPQWSYKTG
810 820 830
WKNGFMPAKA YNPDYKCGDD IPSFGNLPEY Y
Length:831
Mass (Da):95,363
Last modified:April 26, 2005 - v1
Checksum:i9A08532CA04B7B3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490510 mRNA. Translation: ABF50886.1.
AACD01000129 Genomic DNA. Translation: EAA62113.1.
BN001304 Genomic DNA. Translation: CBF79583.1.
RefSeqiXP_680802.1. XM_675710.1.

Genome annotation databases

EnsemblFungiiCADANIAT00000639; CADANIAP00000639; CADANIAG00000639.
GeneIDi2869497.
KEGGiani:AN7533.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490510 mRNA. Translation: ABF50886.1.
AACD01000129 Genomic DNA. Translation: EAA62113.1.
BN001304 Genomic DNA. Translation: CBF79583.1.
RefSeqiXP_680802.1. XM_675710.1.

3D structure databases

ProteinModelPortaliQ5AVZ7.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.
mycoCLAPiEXG5D_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00000639; CADANIAP00000639; CADANIAG00000639.
GeneIDi2869497.
KEGGiani:AN7533.2.

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
InParanoidiQ5AVZ7.
KOiK01210.
OMAiNIITHYG.
OrthoDBiEOG7ZPNTV.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 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 nameiEXGD_EMENI
AccessioniPrimary (citable) accession number: Q5AVZ7
Secondary accession number(s): C8VBL9, Q1HFR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: May 27, 2015
This is version 68 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, 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.