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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: Annotation score: 3 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641Proton donorBy similarity
Active sitei210 – 2101NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate 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
ProteomesiUP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_077840.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 367347Probable endo-beta-1,4-glucanase DPRO_0000394062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi337 ↔ 354By similarity
Disulfide bondi348 ↔ 364By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliB8MXJ7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini329 – 36537CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 235215CatalyticAdd
BLAST
Regioni236 – 32590Ser/Thr-rich linkerAdd
BLAST

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
Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG120437.
HOGENOMiHOG000158937.
OMAiGYIDSPP.
OrthoDBiEOG7KM64H.

Family and domain databases

InterProiIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

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

EnsemblFungiiCADAFLAT00000566; CADAFLAP00000566; CADAFLAG00000566.
GeneIDi7913045.
KEGGiafv:AFLA_077840.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliB8MXJ7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFLAT00000566; CADAFLAP00000566; CADAFLAG00000566.
GeneIDi7913045.
KEGGiafv:AFLA_077840.

Organism-specific databases

EuPathDBiFungiDB:AFLA_077840.

Phylogenomic databases

eggNOGiNOG120437.
HOGENOMiHOG000158937.
OMAiGYIDSPP.
OrthoDBiEOG7KM64H.

Family and domain databases

InterProiIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Aspergillus flavus strain NRRL 3357."
    Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Entry informationi

Entry nameiEGLD_ASPFN
AccessioniPrimary (citable) accession number: B8MXJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: March 3, 2009
Last modified: April 29, 2015
This is version 26 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.