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Protein

Probable endo-beta-1,4-glucanase D

Gene

eglD

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity).By similarity

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei164Proton donorBy similarity1
Active sitei210NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Probable endo-beta-1,4-glucanase D (EC:3.2.1.4)
Short name:
Endoglucanase D
Alternative name(s):
Carboxymethylcellulase D
Cellulase D
Gene namesi
Name:eglD
ORF Names:AFLA_077840
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_077840

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000039406221 – 367Probable endo-beta-1,4-glucanase DAdd BLAST347

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi337 ↔ 354By similarity
Disulfide bondi348 ↔ 364By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiB8MXJ7

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00000566

Structurei

3D structure databases

ProteinModelPortaliB8MXJ7
SMRiB8MXJ7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini329 – 365CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 235CatalyticAdd BLAST215
Regioni236 – 325Ser/Thr-rich linkerAdd BLAST90

Domaini

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 61 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000158937
KOiK19356
OMAiLTFEWYH
OrthoDBiEOG092C48ID

Family and domain databases

InterProiView protein in InterPro
IPR035971 CBD_sf
IPR000254 Cellulose-bd_dom_fun
IPR005103 Glyco_hydro_61
PfamiView protein in Pfam
PF00734 CBM_1, 1 hit
PF03443 Glyco_hydro_61, 1 hit
SMARTiView protein in SMART
SM00236 fCBD, 1 hit
SUPFAMiSSF57180 SSF57180, 1 hit
PROSITEiView protein in PROSITE
PS00562 CBM1_1, 1 hit
PS51164 CBM1_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

B8MXJ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN
60 70 80 90 100
SPITDVTSKD MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS
110 120 130 140 150
SHKGPIMVYM APTEKGTAGN GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT
160 170 180 190 200
VPDVAAGEYL FRPEIIALHE GNRQGGAQFY MECVQVKVTS SGSKTLPEGV
210 220 230 240 250
SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS SPSASASASA
260 270 280 290 300
PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA
310 320 330 340 350
PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE
360
GLTCKKWNPY YYQCISA
Length:367
Mass (Da):38,033
Last modified:March 3, 2009 - v1
Checksum:i0C038474B7C681F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963472 Genomic DNA Translation: EED57089.1
RefSeqiXP_002372701.1, XM_002372660.1

Genome annotation databases

EnsemblFungiiEED57089; EED57089; AFLA_077840
GeneIDi7913045
KEGGiafv:AFLA_077840

Similar proteinsi

Entry informationi

Entry nameiEGLD_ASPFN
AccessioniPrimary (citable) accession number: B8MXJ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: March 3, 2009
Last modified: May 23, 2018
This is version 39 of the entry and version 1 of the sequence. See 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

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