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Protein

Endoglucanase E-5

Gene

celE

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: cellulose degradation

This protein is involved in the pathway cellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway cellulose degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei299Proton donorBy similarity1
Active sitei391NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayi
UPA00696

Protein family/group databases

CAZyiCBM2 Carbohydrate-Binding Module Family 2
GH5 Glycoside Hydrolase Family 5

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E-5 (EC:3.2.1.4)
Alternative name(s):
Cellulase E-5
Cellulase E5
Endo-1,4-beta-glucanase E-4
Gene namesi
Name:celE
OrganismiThermobifida fusca (Thermomonospora fusca)
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Add BLAST36
ChainiPRO_000000786637 – 466Endoglucanase E-5Add BLAST430

Proteomic databases

PRIDEiQ01786

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ01786
SMRiQ01786
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01786

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 139CBM2PROSITE-ProRule annotationAdd BLAST103

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107SMB Bacteria
COG2730 LUCA

Family and domain databases

Gene3Di2.60.40.290, 1 hit
InterProiView protein in InterPro
IPR001919 CBD2
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR012291 CBM2_carb-bd_dom_sf
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00553 CBM_2, 1 hit
PF00150 Cellulase, 1 hit
SMARTiView protein in SMART
SM00637 CBD_II, 1 hit
SUPFAMiSSF49384 SSF49384, 1 hit
SSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51173 CBM2, 1 hit
PS00659 GLYCOSYL_HYDROL_F5, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q01786-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD
60 70 80 90 100
NGYSASVTVR NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT
110 120 130 140 150
GVSWNSTIPP GGTASSGFIA SGSGEPTHCT INGAPCDEGS EPGGPGGPGT
160 170 180 190 200
PSPDPGTQPG TGTPVERYGK VQVCGTQLCD EHGNPVQLRG MSTHGIQWFD
210 220 230 240 250
HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD RMHQLIDMAT
260 270 280 290 300
ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP
310 320 330 340 350
NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA
360 370 380 390 400
ANPVNASNIM YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD
410 420 430 440 450
GANDFQMADR YIDLMAERKI GWTKWNYSDD FRSGAVFQPG TCASGGPWSG
460
SSLKASGQWV RSKLQS
Length:466
Mass (Da):49,801
Last modified:July 15, 1999 - v2
Checksum:i1CF0ADFBF2DEF82E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01577 Genomic DNA Translation: AAC09379.1
PIRiC42360

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01577 Genomic DNA Translation: AAC09379.1
PIRiC42360

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKRX-ray1.77A/B161-466[»]
2CKSX-ray1.60A/B161-466[»]
ProteinModelPortaliQ01786
SMRiQ01786
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2 Carbohydrate-Binding Module Family 2
GH5 Glycoside Hydrolase Family 5

Proteomic databases

PRIDEiQ01786

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107SMB Bacteria
COG2730 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00696

Miscellaneous databases

EvolutionaryTraceiQ01786

Family and domain databases

Gene3Di2.60.40.290, 1 hit
InterProiView protein in InterPro
IPR001919 CBD2
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR012291 CBM2_carb-bd_dom_sf
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00553 CBM_2, 1 hit
PF00150 Cellulase, 1 hit
SMARTiView protein in SMART
SM00637 CBD_II, 1 hit
SUPFAMiSSF49384 SSF49384, 1 hit
SSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS51173 CBM2, 1 hit
PS00659 GLYCOSYL_HYDROL_F5, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGUN5_THEFU
AccessioniPrimary (citable) accession number: Q01786
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 15, 1999
Last modified: May 23, 2018
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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