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Protein

Endoglucanase E-2

Gene

celB

Organism
Thermobifida fusca (Thermomonospora fusca)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 sitei1101
Active sitei148Proton donor1
Active sitei296Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00696.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase E-2 (EC:3.2.1.4)
Alternative name(s):
Cellulase E-2
Cellulase E2
Endo-1,4-beta-glucanase E-2
Gene namesi
Name:celB
OrganismiThermobifida fusca (Thermomonospora fusca)
Taxonomic identifieri2021 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi163E → G: Loss of ability to form dimers. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Tat-type signalPROSITE-ProRule annotation1 PublicationAdd BLAST31
ChainiPRO_000000790932 – 441Endoglucanase E-2Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi111 ↔ 156
Disulfide bondi263 ↔ 298
Disulfide bondi346 ↔ 438Sequence analysis

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi269800.Tfu_1074.

Structurei

Secondary structure

1441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Helixi43 – 50Combined sources8
Helixi57 – 63Combined sources7
Turni64 – 66Combined sources3
Beta strandi71 – 73Combined sources3
Turni78 – 80Combined sources3
Helixi81 – 95Combined sources15
Beta strandi100 – 103Combined sources4
Beta strandi107 – 109Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi119 – 121Combined sources3
Helixi122 – 134Combined sources13
Turni135 – 138Combined sources4
Beta strandi142 – 145Combined sources4
Helixi149 – 153Combined sources5
Helixi158 – 178Combined sources21
Beta strandi183 – 187Combined sources5
Beta strandi191 – 194Combined sources4
Helixi196 – 205Combined sources10
Helixi208 – 211Combined sources4
Beta strandi213 – 218Combined sources6
Helixi225 – 239Combined sources15
Beta strandi245 – 249Combined sources5
Beta strandi274 – 276Combined sources3
Beta strandi283 – 288Combined sources6
Beta strandi297 – 301Combined sources5
Helixi307 – 315Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMLX-ray1.80A32-317[»]
2BODX-ray1.50X32-317[»]
2BOEX-ray1.15X32-317[»]
2BOFX-ray1.64X32-317[»]
2BOGX-ray1.04X32-317[»]
3RPTX-ray1.30A/X33-103[»]
A/X128-145[»]
A/X169-317[»]
ProteinModelPortaliP26222.
SMRiP26222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26222.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini339 – 441CBM2PROSITE-ProRule annotationAdd BLAST103

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 320CatalyticAdd BLAST289
Regioni321 – 340LinkerAdd BLAST20

Sequence similaritiesi

Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108W9Q. Bacteria.
COG5297. LUCA.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN
60 70 80 90 100
NPNDPRTPVI RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI
110 120 130 140 150
LVVYNAPGRD CGNHSSGGAP SHSAYRSWID EFAAGLKNRP AYIIVEPDLI
160 170 180 190 200
SLMSSCMQHV QQEVLETMAY AGKALKAGSS QARIYFDAGH SAWHSPAQMA
210 220 230 240 250
SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG NPSLRAVIDT
260 270 280 290 300
SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA
310 320 330 340 350
GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY
360 370 380 390 400
TIANEWNDGF QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS
410 420 430 440
SVTARNVGHN GTLSQGASTE FGFVGSKGNS NSVPTLTCAA S
Length:441
Mass (Da):45,844
Last modified:February 1, 1996 - v2
Checksum:i87218E4537092AE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73321 mRNA. Translation: AAC06388.1.
PIRiA42360.
T12011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73321 mRNA. Translation: AAC06388.1.
PIRiA42360.
T12011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TMLX-ray1.80A32-317[»]
2BODX-ray1.50X32-317[»]
2BOEX-ray1.15X32-317[»]
2BOFX-ray1.64X32-317[»]
2BOGX-ray1.04X32-317[»]
3RPTX-ray1.30A/X33-103[»]
A/X128-145[»]
A/X169-317[»]
ProteinModelPortaliP26222.
SMRiP26222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269800.Tfu_1074.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH6. Glycoside Hydrolase Family 6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108W9Q. Bacteria.
COG5297. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00696.

Miscellaneous databases

EvolutionaryTraceiP26222.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.40. 1 hit.
InterProiIPR016288. Beta_cellobiohydrolase.
IPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001524. Glyco_hydro_6_CS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PRINTSiPR00733. GLHYDRLASE6.
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51989. SSF51989. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGUN2_THEFU
AccessioniPrimary (citable) accession number: P26222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 122 of the entry and version 2 of the sequence. [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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.