[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=VTT-D-80133; DOI=10.1016/0378-1119(86)90023-5; PubMed=2948877 [NCBI, ExPASy, EBI, Israel, Japan] Penttilae M., Lehtovaara P., Nevalainen H., Bhikhabhai R., Knowles J.K.C.; "Homology between cellulase genes of Trichoderma reesei: complete nucleotide sequence of the endoglucanase I gene."; Gene 45:253-263(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=L27; van Arsdell J.N., Kwok S., Schweickart V.L., Ladner M.B., Gelfand D.H., Innis M.A.; "Cloning, characterization, and expression in Saccharomyces cerevisiae of endoglucanase I from Trichoderma reesei."; Biotechnology (N.Y.) 5:60-64(1987).
[3]	ACTIVE SITE GLU-149. Tomme P., Clayssens M.; "Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei."; FEBS Lett. 243:239-243(1989).
[4]	X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 23-393. DOI=10.1006/jmbi.1997.1243; PubMed=9325098 [NCBI, ExPASy, EBI, Israel, Japan] Kleywegt G.J., Zou J.-Y., Divne C., Davies G.J., Sinning I., Staehlberg J., Reinikainen T., Srisodsuk M., Teeri T.T., Jones T.A.; "The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6-A resolution, and a comparison with related enzymes."; J. Mol. Biol. 272:383-397(1997).

Comments

FUNCTION: 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.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Copyright

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

Cross-references

Sequence databases

EMBL

M15665; AAA34212.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25928; A25928.

3D structure databases

PDB

1EG1; X-ray; 3.60 A; A/C=23-393.

[ExPASy / RCSB / EBI]

PDBsum

1EG1; -.

ModBase

P07981.

Ontologies

GO:0008810;	Molecular function: cellulase activity (inferred from electronic annotation from EC).
GO:0030245;	Biological process: cellulose catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000254; CBD_fun.
IPR001722; Glyco_hydro_7.
Graphical view of domain structure.

Gene3D

G3DSA:2.70.100.10; Glyco_hydro_7; 1.

Pfam

PF00734; CBM_1; 1.
PF00840; Glyco_hydro_7; 1.
Pfam graphical view of domain structure.

PRINTS

PR00734; GLHYDRLASE7.

ProDom

PD186135; Glyco_hydro_7; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00236; fCBD; 1.
SMART graphical view of domain structure.

PROSITE

PS00562; CBM1_1; 1.
PS51164; CBM1_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

P07981; -.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`CHAIN`	`23 459`	`437`	`Endoglucanase EG-1.`	`PRO_0000007915`
`DOMAIN`	`423 459`	`37`	`CBM1.`
`REGION`	`23 397`	`375`	`Catalytic.`
`REGION`	`398 423`	`26`	`Linker.`
`ACT_SITE`	`149 149`
`ACT_SITE`	`218 218`		`Nucleophile.`
`ACT_SITE`	`223 223`		`Proton donor.`
`CARBOHYD`	`78 78`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`164 164`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`204 204`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`208 208`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`394 394`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`431 448`		`By similarity.`
`DISULFID`	`442 458`		`By similarity.`
`STRAND`	`27 29`	`3`
`STRAND`	`38 42`	`5`
`TURN`	`43 45`	`3`
`STRAND`	`46 50`	`5`
`STRAND`	`53 56`	`4`
`HELIX`	`58 60`	`3`
`STRAND`	`70 73`	`4`
`TURN`	`79 81`	`3`
`STRAND`	`83 85`	`3`
`HELIX`	`86 91`	`6`
`TURN`	`99 103`	`5`
`STRAND`	`104 106`	`3`
`STRAND`	`108 115`	`8`
`STRAND`	`120 125`	`6`
`STRAND`	`130 134`	`5`
`STRAND`	`138 140`	`3`
`STRAND`	`148 154`	`7`
`STRAND`	`163 170`	`8`
`TURN`	`174 177`	`4`
`HELIX`	`185 188`	`4`
`STRAND`	`201 203`	`3`
`STRAND`	`218 224`	`7`
`STRAND`	`231 234`	`4`
`TURN`	`250 254`	`5`
`STRAND`	`258 260`	`3`
`STRAND`	`263 265`	`3`
`STRAND`	`271 279`	`9`
`STRAND`	`288 297`	`10`
`STRAND`	`310 312`	`3`
`HELIX`	`317 321`	`5`
`TURN`	`322 324`	`3`
`HELIX`	`325 333`	`9`
`STRAND`	`335 343`	`9`
`TURN`	`345 349`	`5`
`HELIX`	`350 353`	`4`
`HELIX`	`355 357`	`3`
`TURN`	`362 365`	`4`
`HELIX`	`367 373`	`7`
`STRAND`	`378 388`	`11`
`TURN`	`389 391`	`3`

Sequence information

Length: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 48208 Da [This is the MW of the unprocessed precursor]

CRC64: D235A256F808CBB9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPSVTLPLT TAILAIARLV AAQQPGTSTP EVHPKLTTYK CTKSGGCVAQ DTSVVLDWNY 

        70         80         90        100        110        120 
RWMHDANYNS CTVNGGVNTT LCPDEATCGK NCFIEGVDYA ASGVTTSGSS LTMNQYMPSS 

       130        140        150        160        170        180 
SGGYSSVSPR LYLLDSDGEY VMLKLNGQEL SFDVDLSALP CGENGSLYLS QMDENGGANQ 

       190        200        210        220        230        240 
YNTAGANYGS GYCDAQCPVQ TWRNGTLNTS HQGFCCNEMD ILEGNSRANA LTPHSCTATA 

       250        260        270        280        290        300 
CDSAGCGFNP YGSGYKSYYG PGDTVDTSKT FTIITQFNTD NGSPSGNLVS ITRKYQQNGV 

       310        320        330        340        350        360 
DIPSAQPGGD TISSCPSASA YGGLATMGKA LSSGMVLVFS IWNDNSQYMN WLDSGNAGPC 

       370        380        390        400        410        420 
SSTEGNPSNI LANNPNTHVV FSNIRWGDIG STTNSTAPPP PPASSTTFST TRRSSTTSSS 

       430        440        450 
PSCTQTHWGQ CGGIGYSGCK TCTSGTTCQY SNDYYSQCL

P07981 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