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Protein

Endoglucanase-1

Gene
N/A
Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Miscellaneous

Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Protein family/group databases

CAZyiGH12. Glycoside Hydrolase Family 12.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase-1 (EC:3.2.1.4)
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Endoglucanase I
FI-CMCase
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000000801817 – 237Endoglucanase-1Add BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17Pyrrolidone carboxylic acid1 Publication1

Keywords - PTMi

Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP22669.

Expressioni

Inductioni

By cellulosic materials and hemicelluloses.

Structurei

Secondary structure

1237
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 30Combined sources4
Beta strandi33 – 36Combined sources4
Helixi42 – 44Combined sources3
Beta strandi45 – 56Combined sources12
Beta strandi61 – 71Combined sources11
Beta strandi80 – 84Combined sources5
Helixi91 – 93Combined sources3
Beta strandi98 – 106Combined sources9
Beta strandi110 – 123Combined sources14
Beta strandi132 – 142Combined sources11
Beta strandi148 – 157Combined sources10
Beta strandi160 – 169Combined sources10
Beta strandi172 – 178Combined sources7
Beta strandi184 – 189Combined sources6
Helixi191 – 201Combined sources11
Helixi205 – 207Combined sources3
Beta strandi209 – 234Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GM3X-ray1.59A/B19-237[»]
5GM4X-ray1.92A/B/C/D/E/F/G19-237[»]
5GM5X-ray1.73A/B/C/D/E/F/G18-237[»]
ProteinModelPortaliP22669.
SMRiP22669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiView protein in InterPro
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR002594. GH12.
PfamiView protein in Pfam
PF01670. Glyco_hydro_12. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P22669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAFHLLAAL AGAAVAQQAQ LCDQYATYTG GVYTINNNLW GKDAGSGSQC
60 70 80 90 100
TTVNSASSAG TSWSTKWNWS GGENSVKSYA NSGLTFNKKL VSQISQIPTT
110 120 130 140 150
ARWSYDNTGI RADVAYDLFT AADINHVTWS GDYELMIWLA RYGGVQPIGS
160 170 180 190 200
QIATATVDGQ TWELWYGANG SQKTYSFVAP TPITSFQGDV NDFFKYLTQN
210 220 230
HGFPASSQYL ITLQFGTEPF TGGPATLSVS NWSASVQ
Length:237
Mass (Da):25,560
Last modified:August 1, 1991 - v1
Checksum:i8F173571A8AE6931
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00546 Genomic DNA. Translation: BAA00435.1.
X52525 mRNA. Translation: CAA36757.1.
PIRiS12610.

Similar proteinsi

Entry informationi

Entry nameiGUN_ASPAC
AccessioniPrimary (citable) accession number: P22669
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: August 30, 2017
This is version 88 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families