Reviewed, UniProtKB/Swiss-Prot Q9C1S9 (GUX6_HUMIN)

Names and origin

Protein names

Recommended name:
    Exoglucanase-6A
    EC=3.2.1.91
Alternative name(s):
    Exocellobiohydrolase 6A
    1,4-beta-cellobiohydrolase 6A
    Beta-glucancellobiohydrolase 6A
    Avicelase 2

Gene names

Name:	cel6A
Synonyms:	avi2

Organism

Humicola insolens

Taxonomic identifier

34413 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	476 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)

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	Hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 6 (cellulase A) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	cellulose 1,4-beta-cellobiosidase activity Inferred from electronic annotation. Source: EC cellulose 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 – 16

16

Potential

Chain

17 – 476

460

Exoglucanase-6A

PRO_0000248843

Regions

Domain

33 – 60

28

CBM1

Region

200 – 222

23

Substrate binding loop 1

Region

423 – 461

39

Substrate binding loop 2

Compositional bias

73 – 78

6

Poly-Ser

Sites

Active site

252

1

Proton donor

Active site

431

1

Proton acceptor Probable

Binding site

163

1

Substrate

Binding site

165

1

Substrate

Binding site

297

1

Substrate

Binding site

300

1

Substrate

Binding site

336

1

Substrate

Binding site

397

1

Substrate

Binding site

425

1

Substrate

Binding site

429

1

Substrate

Amino acid modifications

Glycosylation

144

1

O-linked (Man...)

Glycosylation

153

1

O-linked (Man...)

Glycosylation

167

1

N-linked (GlcNAc...)

Disulfide bond

33 ↔ 50

Disulfide bond

44 ↔ 60

Secondary structure

1

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476

Helix Strand Turn

Details...

Turn

119 – 122

4

Helix

129 – 137

9

Helix

140 – 142

3

Helix

146 – 155

10

Beta strand

162 – 164

3

Helix

167 – 169

3

Turn

170 – 172

3

Helix

173 – 186

14

Beta strand

193 – 199

7

Beta strand

209 – 211

3

Helix

218 – 220

3

Helix

222 – 239

18

Turn

240 – 242

3

Beta strand

245 – 249

5

Helix

255 – 259

5

Helix

264 – 283

20

Beta strand

289 – 294

6

Turn

298 – 302

5

Helix

304 – 320

17

Beta strand

327 – 333

7

Helix

347 – 349

3

Helix

357 – 370

14

Beta strand

376 – 380

5

Beta strand

385 – 388

4

Beta strand

398 – 402

5

Beta strand

418 – 422

5

Helix

443 – 446

4

Helix

462 – 470

9

Sequences

	Sequence		Length	Mass (Da)
	Q9C1S9-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D2B0054F1381E653	FASTA	476	51,276
	10 20 30 40 50 60 MAKFFLTAAF AAAALAAPVV EERQNCAPTW GQCGGIGFNG PTCCQSGSTC VKQNDWYSQC 70 80 90 100 110 120 LPGSQVTTTS TTSTSSSSTT SRATSTTRTG GVTSITTAPT RTVTIPGGAT TTASYNGNPF 130 140 150 160 170 180 EGVQLWANNY YRSEVHTLAI PQITDPALRA AASAVAEVPS FQWLDRNVTV DTLLVETLSE 190 200 210 220 230 240 IRAANQAGAN PPYAAQIVVY DLPDRDCAAA ASNGEWAIAN NGANNYKGYI NRIREILISF 250 260 270 280 290 300 SDVRTILVIE PDSLANMVTN MNVAKCSGAA STYRELTIYA LKQLDLPHVA MYMDAGHAGW 310 320 330 340 350 360 LGWPANIQPA AELFAKIYED AGKPRAVRGL ATNVANYNAW SISSPPPYTS PNPNYDEKHY 370 380 390 400 410 420 IEAFRPLLEA RGFPAQFIVD QGRSGKQPTG QKEWGHWCNA IGTGFGMRPT ANTGHQYVDA 430 440 450 460 470 FVWVKPGGEC DGTSDTTAAR YDYHCGLEDA LKPAPEAGQW FQAYFEQLLR NANPPF

References

[1]	"Cloning and overexpression of the avi2 gene encoding a major cellulase produced by Humicola insolens FERM BP-5977." Moriya T., Watanabe M., Sumida N., Okakura K., Murakami T. Biosci. Biotechnol. Biochem. 67:1434-1437(2003) [PubMed: 12843680] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FERM BP-5977.
[2]	"Enzymatic properties of cellulases from Humicola insolens." Schuelein M. J. Biotechnol. 57:71-81(1997) [PubMed: 9335167] [Abstract] Cited for: CATALYTIC ACTIVITY.
[3]	"Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding." Varrot A., Schuelein M., Davies G.J. Biochemistry 38:8884-8891(1999) [PubMed: 10413461] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 115-476 IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE, ACTIVE SITE, GLYCOSYLATION AT ASN-167.
[4]	"Structure of the Humicola insolens cellobiohydrolase Cel6A D416A mutant in complex with a non-hydrolysable substrate analogue, methyl cellobiosyl-4-thio-beta-cellobioside, at 1.9 A." Varrot A., Frandsen T.P., Driguez H., Davies G.J. Acta Crystallogr. D 58:2201-2204(2002) [PubMed: 12454501] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-476 OF MUTANT ALA-416 IN COMPLEX WITH SUBSTRATE ANALOG, GLYCOSYLATION AT ASN-167.
[5]	"Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens." Varrot A., Frandsen T.P., von Ossowski I., Boyer V., Cottaz S., Driguez H., Schuelein M., Davies G.J. Structure 11:855-864(2003) [PubMed: 12842048] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 113-476 OF MUTANT ASN-431 IN COMPLEX WITH SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-167.
[6]	"Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution." Varrot A., Hastrup S., Schuelein M., Davies G.J. Biochem. J. 337:297-304(1999) [PubMed: 9882628] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-476, FUNCTION, SUBUNIT, GLYCOSYLATION AT THR-144; SER-153 AND ASN-167.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB048710 Genomic DNA. Translation: BAB39154.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BVW	X-ray	1.92	A	117-476	[»]
1GZ1	X-ray	1.90	A	115-476	[»]
1OC5	X-ray	1.70	A	113-476	[»]
1OC6	X-ray	1.50	A	113-476	[»]
1OC7	X-ray	1.11	A	113-476	[»]
1OCB	X-ray	1.75	A/B	115-476	[»]
1OCJ	X-ray	1.30	A	115-476	[»]
1OCN	X-ray	1.31	A	115-476	[»]
2BVW	X-ray	1.70	A/B	115-476	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR016288. Beta_cellobiohydrolase.
IPR000254. CBD_fun.
IPR001524. Glyco_hydro_6.
[Graphical view]

Gene3D

G3DSA:3.20.20.40. Glyco_hydro_6. 1 hit.

Pfam

PF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]

PIRSF

PIRSF001100. Beta_cellobiohydrolase. 1 hit.

PRINTS

PR00733. GLHYDRLASE6.

ProDom

PD001821. CBD_fungal. 1 hit.
PD003733. Glyco_hydro_6. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00236. fCBD. 1 hit.
[Graphical view]

PROSITE

PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q9C1S9.

Entry information

Entry name

GUX6_HUMIN

Accession

Primary (citable) accession number: Q9C1S9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	June 1, 2001
Last modified:	November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)