UniProtKB - Q01786 (GUN5_THEFU)
Protein
Endoglucanase E-5
Gene
celE
Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Functioni
Catalytic activityi
- Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. EC:3.2.1.4
: cellulose degradation Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 299 | Proton donorBy similarity | 1 | |
Active sitei | 391 | NucleophileBy similarity | 1 |
GO - Molecular functioni
- cellulase activity Source: UniProtKB-EC
- polysaccharide binding Source: InterPro
GO - Biological processi
- cellulose catabolic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation |
Enzyme and pathway databases
UniPathwayi | UPA00696 |
Protein family/group databases
CAZyi | CBM2, 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 |
Organismi | Thermobifida fusca (Thermomonospora fusca) |
Taxonomic identifieri | 2021 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Streptosporangiales › Nocardiopsaceae › Thermobifida |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 36 | Add BLAST | 36 | |
ChainiPRO_0000007866 | 37 – 466 | Endoglucanase E-5Add BLAST | 430 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q01786 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q01786 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 37 – 139 | CBM2PROSITE-ProRule annotationAdd BLAST | 103 |
Sequence similaritiesi
Belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 2.60.40.290, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00553, CBM_2, 1 hit PF00150, Cellulase, 1 hit |
SMARTi | View protein in SMART SM00637, CBD_II, 1 hit |
SUPFAMi | SSF49384, SSF49384, 1 hit SSF51445, SSF51445, 1 hit |
PROSITEi | View protein in PROSITE PS51173, CBM2, 1 hit PS00659, GLYCOSYL_HYDROL_F5, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q01786-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L01577 Genomic DNA Translation: AAC09379.1 |
PIRi | C42360 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L01577 Genomic DNA Translation: AAC09379.1 |
PIRi | C42360 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2CKR | X-ray | 1.77 | A/B | 161-466 | [»] | |
2CKS | X-ray | 1.60 | A/B | 161-466 | [»] | |
SMRi | Q01786 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
CAZyi | CBM2, Carbohydrate-Binding Module Family 2 GH5, Glycoside Hydrolase Family 5 |
Enzyme and pathway databases
UniPathwayi | UPA00696 |
Miscellaneous databases
EvolutionaryTracei | Q01786 |
Family and domain databases
Gene3Di | 2.60.40.290, 1 hit |
InterProi | View 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 |
Pfami | View protein in Pfam PF00553, CBM_2, 1 hit PF00150, Cellulase, 1 hit |
SMARTi | View protein in SMART SM00637, CBD_II, 1 hit |
SUPFAMi | SSF49384, SSF49384, 1 hit SSF51445, SSF51445, 1 hit |
PROSITEi | View protein in PROSITE PS51173, CBM2, 1 hit PS00659, GLYCOSYL_HYDROL_F5, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GUN5_THEFU | |
Accessioni | Q01786Primary (citable) accession number: Q01786 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | July 15, 1999 | |
Last modified: | April 7, 2021 | |
This is version 111 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families