Q01786 (GUN5_THEFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

celE

Organism

Thermomonospora fusca

Taxonomic identifier

2021 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	466 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.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) 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-UniPathway
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 – 36

36

Chain

37 – 466

430

Endoglucanase E-5

PRO_0000007866

Regions

Domain

37 – 139

103

CBM2

Sites

Active site

299

1

Proton donor By similarity

Active site

391

1

Nucleophile By similarity

Secondary structure

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466

Helix Strand Turn

Details...

Helix

164 – 168

5

Beta strand

172 – 174

3

Beta strand

177 – 179

3

Beta strand

189 – 192

4

Helix

196 – 199

4

Helix

200 – 202

3

Helix

205 – 213

9

Beta strand

218 – 227

10

Helix

231 – 233

3

Helix

235 – 250

16

Turn

251 – 253

3

Beta strand

255 – 261

7

Helix

268 – 271

4

Helix

272 – 286

15

Beta strand

290 – 295

6

Helix

305 – 322

18

Beta strand

328 – 330

3

Helix

333 – 336

4

Helix

340 – 342

3

Helix

347 – 351

5

Beta strand

357 – 366

10

Turn

367 – 369

3

Helix

372 – 384

13

Beta strand

387 – 395

9

Helix

405 – 418

14

Beta strand

422 – 425

4

Beta strand

435 – 437

3

Helix

441 – 444

4

Helix

450 – 452

3

Helix

455 – 465

11

Sequences

	Sequence		Length	Mass (Da)
	Q01786 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 1CF0ADFBF2DEF82E	FASTA	466	49,801
	10 20 30 40 50 60 MAKSPAARKG XPPVAVAVTA ALALLIALLS PGVAQAAGLT ATVTKESSWD NGYSASVTVR 70 80 90 100 110 120 NDTSSTVSQW EVVLTLPGGT TVAQVWNAQH TSSGNSHTFT GVSWNSTIPP GGTASSGFIA 130 140 150 160 170 180 SGSGEPTHCT INGAPCDEGS EPGGPGGPGT PSPDPGTQPG TGTPVERYGK VQVCGTQLCD 190 200 210 220 230 240 EHGNPVQLRG MSTHGIQWFD HCLTDSSLDA LAYDWKADII RLSMYIQEDG YETNPRGFTD 250 260 270 280 290 300 RMHQLIDMAT ARGLYVIVDW HILTPGDPHY NLDRAKTFFA EIAQRHASKT NVLYEIANEP 310 320 330 340 350 360 NGVSWASIKS YAEEVIPVIR QRDPDSVIIV GTRGWSSLGV SEGSGPAEIA ANPVNASNIM 370 380 390 400 410 420 YAFHFYAASH RDNYLNALRE ASELFPVFVT EFGTETYTGD GANDFQMADR YIDLMAERKI 430 440 450 460 GWTKWNYSDD FRSGAVFQPG TCASGGPWSG SSLKASGQWV RSKLQS

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YX.
[2]	Lao G., Ghangas G.S., Jung E.D., Wilson D.B. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Activity studies of eight purified cellulases: specificity, synergism, and binding domain effects." Irwin D.C., Spezio M., Walker L.P., Wilson D.B. Biotechnol. Bioeng. 42:1002-1013(1993) Cited for: PROTEIN SEQUENCE OF 137-142 AND 157-166. Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L01577 Genomic DNA. Translation: AAC09379.1.

PIR

C42360.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q01786.

SMR

Q01786. Positions 161-466.

ModBase

Search...

Protein family/group databases

CAZy

CBM2. Carbohydrate-Binding Module Family 2.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00696.

Family and domain databases

Gene3D

2.60.40.290. 1 hit.
3.20.20.80. 1 hit.

InterPro

IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF00553. CBM_2. 1 hit.
PF00150. Cellulase. 1 hit.
[Graphical view]

SMART

SM00637. CBD_II. 1 hit.
[Graphical view]

SUPFAM

SSF49384. Cellul_bind. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51173. CBM2. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q01786.

Entry information

Entry name

GUN5_THEFU

Accession

Primary (citable) accession number: Q01786

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 15, 1999
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program