Reviewed, UniProtKB/Swiss-Prot Q7SIG5 (GUN6_HUMIN)

Names and origin

Protein names

Recommended name:
    Endoglucanase-6B
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase 6B
    Cellulase 6B

Gene names

Name:

cel6B

Organism

Humicola insolens

Taxonomic identifier

34413 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Humicola

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a central role in the recycling of plant biomass. The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.1
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the glycosyl hydrolase 6 (cellulase B) family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Endoglucanase-6B

PRO_0000248842

Sites

Active site

92

1

Proton donor Potential Ref.2

Active site

139

1

Proton donor Ref.2

Binding site

52

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

54

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

183

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

186

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

222

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

282

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

310

1

Substrate By similarity UniProtKB Q9C1S9

Binding site

314

1

Substrate By similarity UniProtKB Q9C1S9

Secondary structure

1

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348

Helix Strand Turn

Details...

Turn

5 – 8

4

Helix

15 – 29

15

Turn

30 – 32

3

Helix

34 – 46

13

Beta strand

51 – 53

3

Helix

57 – 59

3

Helix

60 – 74

15

Beta strand

79 – 85

7

Helix

93 – 95

3

Beta strand

99 – 101

3

Helix

104 – 106

3

Helix

108 – 115

8

Helix

117 – 126

10

Beta strand

132 – 136

5

Helix

140 – 146

7

Helix

150 – 169

20

Beta strand

175 – 180

6

Helix

184 – 187

4

Helix

190 – 192

3

Helix

193 – 207

15

Beta strand

215 – 218

4

Helix

233 – 235

3

Helix

243 – 255

13

Turn

256 – 258

3

Beta strand

262 – 266

5

Beta strand

268 – 271

4

Beta strand

286 – 289

4

Beta strand

294 – 296

3

Beta strand

303 – 307

5

Beta strand

316 – 318

3

Helix

332 – 340

9

Sequences

	Sequence		Length	Mass (Da)
	Q7SIG5-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 5F1E4A4367402E54	FASTA	348	37,753
	10 20 30 40 50 60 QSGNPFSGRT LLVNSDYSSK LDQTRQAFLS RGDQTNAAKV KYVQEKVGTF YWISNIFLLR 70 80 90 100 110 120 DIDVAIQNAR AAKARGENPI VGLVLYNLPD RDCSAGESSG ELKLSQNGLN RYKNEYVNPF 130 140 150 160 170 180 AQKLKAASDV QFAVILEPDA IGNMVTGTSA FCRNARGPQQ EAIGYAISQL QASHIHLYLD 190 200 210 220 230 240 VANGGWLGWA DKLEPTAQEV ATILQKAGNN AKIRGFSSNV SNYNPYSTSN PPPYTSGSPS 250 260 270 280 290 300 PDESRYATNI ANAMRQRGLP TQFIIDQSRV ALSGARSEWG QWCNVNPAGF GQPFTTNTNN 310 320 330 340 PNVDAIVWVK PGGESDGQCG MGGAPAAGMW FDAYAQMLTQ NAHDEIAR

References

[1]	"Enzymatic properties of cellulases from Humicola insolens." Schuelein M. J. Biotechnol. 57:71-81(1997) [PubMed: 9335167] [Abstract] Cited for: CATALYTIC ACTIVITY.
[2]	"Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution." Davies G.J., Brzozowski A.M., Dauter M., Varrot A., Schuelein M. Biochem. J. 348:201-207(2000) [PubMed: 10794732] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, ACTIVE SITE.

Cross-references

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DYS	X-ray	1.60	A/B	1-348	[»]

DisProt

DP00283.

ModBase

Search...

Protein family/group databases

CAZy

GH6. Glycoside Hydrolase Family 6.

Enzyme and pathway databases

BRENDA

3.2.1.4. 1892.

Family and domain databases

InterPro

IPR016288. Beta_cellobiohydrolase.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.40. Glyco_hydro_6. 1 hit.

Pfam

PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]

PIRSF

PIRSF001100. Beta_cellobiohydrolase. 1 hit.

PRINTS

PR00733. GLHYDRLASE6.

ProDom

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

PROSITE

PS00655. GLYCOSYL_HYDROL_F6_1. False negative.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GUN6_HUMIN

Accession

Primary (citable) accession number: Q7SIG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	December 15, 2003
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)