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A2RAR6

- EXGA_ASPNC

UniProt

A2RAR6 - EXGA_ASPNC

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Protein

Probable glucan 1,3-beta-glucosidase A

Gene

exgA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101Proton donorBy similarity
Active sitei308 – 3081NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cell wall biogenesis/degradation, Polysaccharide degradation

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable glucan 1,3-beta-glucosidase A (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 1
Exo-1,3-beta-glucanase A
Gene namesi
Name:exgA
Synonyms:exg1
ORF Names:An18g04100
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 8L

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 416394Probable glucan 1,3-beta-glucosidase APRO_5000221332Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi290 ↔ 415By similarity
Disulfide bondi316 ↔ 342By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi5061.CADANGAP00013786.

Structurei

3D structure databases

ProteinModelPortaliA2RAR6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
KOiK01210.
OrthoDBiEOG7JT75H.

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.

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

A2RAR6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFVESAKKAL LALSLLAASA QAVPRVRRQG ASSSFDYKSQ IVRGVNLGGW
60 70 80 90 100
LVTEPWITPS LYDSTGGGAV DEWTLCQILG KDEAQAKLSS HWSSFITQSD
110 120 130 140 150
FDRMAQAGLN HVRIPIGYWA VAPIDGEPYV SGQIDYLDQA VTWARAAGLK
160 170 180 190 200
VLVDLHGAPG SQNGFDNSGH RGPIQWQQGD TVNQTMTAFD ALARRYAQSD
210 220 230 240 250
TVTAIEAVNE PNIPGGVNED GLKNYYYGAL ADVQRLNPST TLFMSDGFQP
260 270 280 290 300
VESWNGFMQG SNVVMDTHHY QVFDTGLLSM SIDDHVKTAC SLATQHTMQS
310 320 330 340 350
DKPVVVGEWT GALTDCAKYL NGVGNAARYD GTYMSTTKYG DCTGKSTGSV
360 370 380 390 400
ADFSADEKAN TRRYIEAQLE AYEMKSGWLF WTWKTEGAPG WDMQDLLANQ
410
LFPTSPTDRQ YPHQCS
Length:416
Mass (Da):45,526
Last modified:March 6, 2007 - v1
Checksum:i9FC5AADB23A03E24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270406 Genomic DNA. Translation: CAK43212.1.
RefSeqiXP_001398868.1. XM_001398831.2.

Genome annotation databases

EnsemblFungiiCADANGAT00014047; CADANGAP00013786; CADANGAG00014047.
GeneIDi4989974.
KEGGiang:ANI_1_534164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270406 Genomic DNA. Translation: CAK43212.1 .
RefSeqi XP_001398868.1. XM_001398831.2.

3D structure databases

ProteinModelPortali A2RAR6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00013786.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00014047 ; CADANGAP00013786 ; CADANGAG00014047 .
GeneIDi 4989974.
KEGGi ang:ANI_1_534164.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000114462.
KOi K01210.
OrthoDBi EOG7JT75H.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiEXGA_ASPNC
AccessioniPrimary (citable) accession number: A2RAR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: March 6, 2007
Last modified: November 26, 2014
This is version 47 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