Reviewed, UniProtKB/Swiss-Prot P26222 (GUN2_THEFU)

Names and origin

Protein names

Recommended name:
    Endoglucanase E-2
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase E-2
    Cellulase E-2
    Cellulase E2

Gene names

Name:

celB

Organism

Thermomonospora fusca

Taxonomic identifier

2021 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pathway	Glycan metabolism; cellulose degradation.
Subunit structure	Homodimer.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence similarities	Belongs to the glycosyl hydrolase 6 (cellulase B) family. Contains 1 CBM2 (carbohydrate binding type-2) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cellulase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Tat-type signal

Chain

32 – 441

410

Endoglucanase E-2

PRO_0000007909

Regions

Domain

339 – 441

103

CBM2

Region

32 – 320

289

Catalytic

Region

321 – 340

20

Linker

Sites

Active site

110

1

Active site

148

1

Proton donor

Active site

296

1

Nucleophile

Amino acid modifications

Disulfide bond

111 ↔ 156

Disulfide bond

263 ↔ 298

Disulfide bond

346 ↔ 438

Potential

Experimental info

Mutagenesis

163

1

E → G: Loss of ability to form dimers

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

441

Helix Strand Turn

Details...

Helix

43 – 50

8

Helix

57 – 63

7

Turn

64 – 66

3

Beta strand

71 – 73

3

Turn

78 – 80

3

Helix

81 – 95

15

Beta strand

100 – 103

4

Beta strand

119 – 121

3

Helix

122 – 134

13

Turn

135 – 138

4

Beta strand

141 – 145

5

Helix

149 – 153

5

Helix

158 – 178

21

Beta strand

182 – 187

6

Beta strand

191 – 194

4

Helix

196 – 205

10

Helix

208 – 211

4

Beta strand

213 – 218

6

Helix

225 – 239

15

Beta strand

245 – 249

5

Beta strand

274 – 276

3

Beta strand

283 – 288

6

Beta strand

297 – 301

5

Helix

307 – 315

9

Sequences

	Sequence		Length	Mass (Da)
	P26222-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 87218E4537092AE5	FASTA	441	45,844
	10 20 30 40 50 60 MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI 70 80 90 100 110 120 RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP 130 140 150 160 170 180 SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS 190 200 210 220 230 240 QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG 250 260 270 280 290 300 NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA 310 320 330 340 350 360 GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF 370 380 390 400 410 420 QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE 430 440 FGFVGSKGNS NSVPTLTCAA S

References

[1]	"DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca." Lao G., Ghangas G.S., Jung E.D., Wilson D.B. J. Bacteriol. 173:3397-3407(1991) [PubMed: 1904434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YX.
[2]	Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B. Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION. Strain: YX.
[3]	"Cellulases of Thermomonospora fusca." Wilson D.B. Methods Enzymol. 160:314-323(1988) Cited for: PROTEIN SEQUENCE OF 32-47.
[4]	"Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2." McGinnis K., Kroupis C., Wilson D.B. Biochemistry 32:8146-8150(1993) [PubMed: 8347613] [Abstract] Cited for: SUBUNIT, MUTAGENESIS OF GLU-163.
[5]	"Crystal structure of the catalytic domain of a thermophilic endocellulase." Spezio M., Wilson D.B., Karplus P.A. Biochemistry 32:9906-9916(1993) [PubMed: 8399160] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M73321 mRNA. Translation: AAC06388.1.

PIR

A42360.
T12011.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TML	X-ray	1.80	A	32-317	[»]
2BOD	X-ray	1.50	X	32-317	[»]
2BOE	X-ray	1.15	X	32-317	[»]
2BOF	X-ray	1.64	X	32-317	[»]
2BOG	X-ray	1.04	X	32-317	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001919. CBD_bac.
IPR012291. CBD_carb_bd.
IPR001524. Glyco_hydro_6.
[Graphical view]

Gene3D

G3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
G3DSA:3.20.20.40. Glyco_hydro_6. 1 hit.

Pfam

PF00553. CBM_2. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]

PRINTS

PR00733. GLHYDRLASE6.

ProDom

PD003733. Glyco_hydro_6. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00637. CBD_II. 1 hit.
[Graphical view]

PROSITE

PS51173. 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]

ProtoNet

Search...

Other Resources

LinkHub

P26222.

Entry information

Entry name

GUN2_THEFU

Accession

Primary (citable) accession number: P26222

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)