[1]	CATALYTIC ACTIVITY. DOI=10.1016/S0168-1656(97)00090-4; PubMed=9335167 [NCBI, ExPASy, EBI, Israel, Japan] Schuelein M.; "Enzymatic properties of cellulases from Humicola insolens."; J. Biotechnol. 57:71-81(1997).
[2]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT, AND ACTIVE SITE. DOI=10.1042/0264-6021:3480201; PubMed=10794732 [NCBI, ExPASy, EBI, Israel, Japan] Davies G.J., Brzozowski A.M., Dauter M., Varrot A., Schuelein M.; "Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution."; Biochem. J. 348:201-207(2000).

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.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

1DYS; X-ray; 1.60 A; A/B=1-348.

[ExPASy / RCSB / EBI]

1DYS; -.

DP00283; -.

Ontologies

GO:0008810;	Molecular function: cellulase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016288; Beta_cellobiohydrolase.
IPR001524; Glyco_hydro_6.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.40; Glyco_hydro_6; 1.

Pfam

PF01341; Glyco_hydro_6; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001100; Beta_cellobiohydrolase; 1.

PRINTS

PR00733; GLHYDRLASE6.

ProDom

PD003733; Glyco_hydro_6; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00655; GLYCOSYL_HYDROL_F6_1; FALSE_NEG.
PS00656; GLYCOSYL_HYDROL_F6_2; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 348`	`348`	`Endoglucanase-6B.`	`PRO_0000248842`
`ACT_SITE`	`92 92`		`Proton donor (Potential).`
`ACT_SITE`	`139 139`		`Proton donor.`
`BINDING`	`52 52`		`Substrate (By similarity).`
`BINDING`	`54 54`		`Substrate (By similarity).`
`BINDING`	`183 183`		`Substrate (By similarity).`
`BINDING`	`186 186`		`Substrate (By similarity).`
`BINDING`	`222 222`		`Substrate (By similarity).`
`BINDING`	`282 282`		`Substrate (By similarity).`
`BINDING`	`310 310`		`Substrate (By similarity).`
`BINDING`	`314 314`		`Substrate (By similarity).`
`TURN`	`5 8`	`4`
`HELIX`	`15 29`	`15`
`TURN`	`30 32`	`3`
`HELIX`	`34 46`	`13`
`STRAND`	`51 53`	`3`
`HELIX`	`57 59`	`3`
`HELIX`	`60 74`	`15`
`STRAND`	`79 85`	`7`
`HELIX`	`93 95`	`3`
`STRAND`	`99 101`	`3`
`HELIX`	`104 106`	`3`
`HELIX`	`108 115`	`8`
`HELIX`	`117 126`	`10`
`STRAND`	`132 136`	`5`
`HELIX`	`140 146`	`7`
`HELIX`	`150 169`	`20`
`STRAND`	`175 180`	`6`
`HELIX`	`184 187`	`4`
`HELIX`	`190 192`	`3`
`HELIX`	`193 207`	`15`
`STRAND`	`215 218`	`4`
`HELIX`	`233 235`	`3`
`HELIX`	`243 255`	`13`
`TURN`	`256 258`	`3`
`STRAND`	`262 266`	`5`
`STRAND`	`268 271`	`4`
`STRAND`	`286 289`	`4`
`STRAND`	`294 296`	`3`
`STRAND`	`303 307`	`5`
`STRAND`	`316 318`	`3`
`HELIX`	`332 340`	`9`

Sequence information

Length: 348 AA [This is the length of the unprocessed precursor]

Molecular weight: 37753 Da [This is the MW of the unprocessed precursor]

CRC64: 5F1E4A4367402E54 [This is a checksum on the sequence]

        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

Q7SIG5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools