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A2QX52

- EXGD_ASPNC

UniProt

A2QX52 - EXGD_ASPNC

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Protein

Probable glucan 1,3-beta-glucosidase D

Gene

exgD

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

Functioni

Glucosidase involved in the degradation of cellulosic biomass. Active on lichenan (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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei597 – 5971Proton donorBy similarity
Active sitei702 – 7021NucleophileBy similarity

GO - Molecular functioni

  1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

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

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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:An11g07660
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 7R

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 830830Probable glucan 1,3-beta-glucosidase DPRO_0000395165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi558 – 5581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi610 – 6101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi669 – 6691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00008917.

Structurei

3D structure databases

ProteinModelPortaliA2QX52.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 307307CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini329 – 830502ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei308 – 32821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 8548Asp-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000114462.
KOiK01210.
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.

A2QX52-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGHSRSRDR LSPSSELDDA DPVYSPSVYQ REHYYNNDSL FDSADDDYTR
60 70 80 90 100
TPRNVYSYET HDEYHDDDDD DDDVHEHDHD HEYDDKFEEP WVPLRAQVEG
110 120 130 140 150
DQWREGFETA IPKEEDVTQA KEYQYQMSGA LGDDGPPPLP SDALGRGKGK
160 170 180 190 200
KRLDRETRRQ RRKERLAAFF KHKNGSASAG LVSGDALAKL LGSQDGDEDC
210 220 230 240 250
LSHLGTERAD SMSQKNLEGG RQRKLPVLSE EPMMLRPFPA VAPTGQTQGR
260 270 280 290 300
VVSGAQLEEG GPGMEMRHRG GGGPPAEGLL QKEGDWDGST KGSSTSARPS
310 320 330 340 350
FWKRYHKTFI FFAILIVLAA IAIPVGIIEA RRLHGTSGGD NSSNSNLKGI
360 370 380 390 400
SRDSIPAYAR GTYLDPFTWY DTTDFNVTFT NATVGGLSIM GLNSTWNDSA
410 420 430 440 450
QANENVPPLN EKFPYGSQPI RGVNLGGWLS IEPFIVPSLF DTYTSSEGII
460 470 480 490 500
DEWTLSEKLG DSAASVIEKH YATFITEQDF ADIRDAGLDH VRIQFSYWAI
510 520 530 540 550
KTYDGDPYVP KIAWRYLLRA IEYCRKYGLR VNLDPHGIPG SQNGWNHSGR
560 570 580 590 600
QGTIGWLNGT DGELNRQRSL EMHDQLSQFF AQDRYKNVVT IYGLVNEPLM
610 620 630 640 650
LSLPVEKVLN WTTEATNLVQ KNGIKAWVTV HDGFLNLDKW DKMLKTRPSN
660 670 680 690 700
MMLDTHQYTV FNTGEIVLNH TRRVELICES WYSMIQQINI TSTGWGPTIC
710 720 730 740 750
GEWSQADTDC AQYVNNVGRG TRWEGTFSLT DSTQYCPTAS EGTCSCTQAN
760 770 780 790 800
AVPGVYSEGY KTFLQTYAEA QMSAFESAMG WFYWTWATES AAQWSYRTAW
810 820 830
KNGYMPKKAY SPSFKCGDTI PSFGNLPEYY
Length:830
Mass (Da):93,303
Last modified:March 6, 2007 - v1
Checksum:iE07B09114631E566
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270244 Genomic DNA. Translation: CAK45960.1.
RefSeqiXP_001394735.1. XM_001394698.1.

Genome annotation databases

EnsemblFungiiCADANGAT00009088; CADANGAP00008917; CADANGAG00009088.
GeneIDi4984985.
KEGGiang:ANI_1_2268094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270244 Genomic DNA. Translation: CAK45960.1 .
RefSeqi XP_001394735.1. XM_001394698.1.

3D structure databases

ProteinModelPortali A2QX52.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00008917.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00009088 ; CADANGAP00008917 ; CADANGAG00009088 .
GeneIDi 4984985.
KEGGi ang:ANI_1_2268094.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000114462.
KOi K01210.
OrthoDBi EOG7ZPNTV.

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 nameiEXGD_ASPNC
AccessioniPrimary (citable) accession number: A2QX52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 43 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