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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: 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)DescriptionActionsGraphical viewLength
Active sitei597Proton donorBy similarity1
Active sitei702NucleophileBy similarity1

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.

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
Proteomesi
  • UP000006706 Componenti: Chromosome 7R

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 307CytoplasmicSequence analysisAdd BLAST307
Transmembranei308 – 328Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini329 – 830ExtracellularSequence analysisAdd BLAST502

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003951651 – 830Probable glucan 1,3-beta-glucosidase DAdd BLAST830

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi341N-linked (GlcNAc...)Sequence analysis1
Glycosylationi376N-linked (GlcNAc...)Sequence analysis1
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1
Glycosylationi393N-linked (GlcNAc...)Sequence analysis1
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1
Glycosylationi546N-linked (GlcNAc...)Sequence analysis1
Glycosylationi558N-linked (GlcNAc...)Sequence analysis1
Glycosylationi610N-linked (GlcNAc...)Sequence analysis1
Glycosylationi669N-linked (GlcNAc...)Sequence analysis1
Glycosylationi689N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA2QX52.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi38 – 85Asp-richAdd BLAST48

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000114462.
KOiK01210.
OrthoDBiEOG092C22A6.

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:
EMBLi
GenBanki
DDBJi
Links Updated
AM270244 Genomic DNA. Translation: CAK45960.1.
RefSeqiXP_001394735.1. XM_001394698.1.

Genome annotation databases

EnsemblFungiiCAK45960; CAK45960; An11g07660.
GeneIDi4984985.
KEGGiang:ANI_1_2268094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270244 Genomic DNA. Translation: CAK45960.1.
RefSeqiXP_001394735.1. XM_001394698.1.

3D structure databases

ProteinModelPortaliA2QX52.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAK45960; CAK45960; An11g07660.
GeneIDi4984985.
KEGGiang:ANI_1_2268094.

Phylogenomic databases

HOGENOMiHOG000114462.
KOiK01210.
OrthoDBiEOG092C22A6.

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...

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: November 30, 2016
This is version 52 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

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 one 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.