[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=YX; PubMed=1904434 [NCBI, ExPASy, EBI, Israel, Japan] Lao G., Ghangas G.S., Jung E.D., Wilson D.B.; "DNA sequences of three beta-1,4-endoglucanase genes from Thermomonospora fusca."; J. Bacteriol. 173:3397-3407(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=YX; Jung E.D., Lao G., Irwin D., Barr B., Benjamin A., Wilson D.B.; Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 32-47. Wilson D.B.; "Cellulases of Thermomonospora fusca."; Methods Enzymol. 160:314-323(1988).
[4]	SUBUNIT, AND MUTAGENESIS OF GLU-163. DOI=10.1021/bi00083a013; PubMed=8347613 [NCBI, ExPASy, EBI, Israel, Japan] McGinnis K., Kroupis C., Wilson D.B.; "Dimerization of Thermomonospora fusca beta-1,4-endoglucanase E2."; Biochemistry 32:8146-8150(1993).
[5]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 32-317. DOI=10.1021/bi00089a006; PubMed=8399160 [NCBI, ExPASy, EBI, Israel, Japan] Spezio M., Wilson D.B., Karplus P.A.; "Crystal structure of the catalytic domain of a thermophilic endocellulase."; Biochemistry 32:9906-9916(1993).

Comments

CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
PATHWAY: Glycan metabolism; cellulose degradation .
SUBUNIT: Homodimer.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
SIMILARITY: Contains 1 CBM2 (carbohydrate binding type-2) 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

M73321; AAC06388.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A42360; A42360.
T12011; T12011.

3D structure databases

PDB

1TML; X-ray; 1.80 A; A=32-317.	[ExPASy / RCSB / EBI]
2BOD; X-ray; 1.50 A; X=32-317.	[ExPASy / RCSB / EBI]
2BOE; X-ray; 1.15 A; X=32-317.	[ExPASy / RCSB / EBI]
2BOF; X-ray; 1.64 A; X=32-317.	[ExPASy / RCSB / EBI]
2BOG; X-ray; 1.04 A; X=32-317.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1TML; -.
2BOD; -.
2BOE; -.
2BOF; -.
2BOG; -.

ModBase

P26222.

Ontologies

GO:0008810;	Molecular function: cellulase activity (inferred from electronic annotation from EC).
GO:0030247;	Molecular function: polysaccharide binding (inferred from electronic annotation from InterPro).
GO:0030245;	Biological process: cellulose catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001919; CBD_bac.
IPR012291; CBD_carb_bd.
IPR001524; Glyco_hydro_6.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.290; CBD_carb_bd; 1.
G3DSA:3.20.20.40; Glyco_hydro_6; 1.

Pfam

PF00553; CBM_2; 1.
PF01341; Glyco_hydro_6; 1.
Pfam graphical view of domain structure.

PRINTS

PR00733; GLHYDRLASE6.

ProDom

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

SMART

SM00637; CBD_II; 1.
SMART graphical view of domain structure.

PROSITE

PS51173; CBM2; 1.
PS00561; CBM2_A; 1.
PS00655; GLYCOSYL_HYDROL_F6_1; 1.
PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Other

P26222; -.

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

Keywords

3D-structure; Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Tat-type signal.`
`CHAIN`	`32 441`	`410`	`Endoglucanase E-2.`	`PRO_0000007909`
`DOMAIN`	`339 441`	`103`	`CBM2.`
`REGION`	`32 320`	`289`	`Catalytic.`
`REGION`	`321 340`	`20`	`Linker.`
`ACT_SITE`	`110 110`
`ACT_SITE`	`148 148`		`Proton donor.`
`ACT_SITE`	`296 296`		`Nucleophile.`
`DISULFID`	`111 156`
`DISULFID`	`263 298`
`DISULFID`	`346 438`		`Potential.`
`MUTAGEN`	`163 163`		`E->G: Loss of ability to form dimers.`
`HELIX`	`43 50`	`8`
`HELIX`	`57 63`	`7`
`TURN`	`64 66`	`3`
`STRAND`	`71 73`	`3`
`TURN`	`78 80`	`3`
`HELIX`	`81 95`	`15`
`STRAND`	`100 103`	`4`
`STRAND`	`119 121`	`3`
`HELIX`	`122 134`	`13`
`TURN`	`135 138`	`4`
`STRAND`	`141 145`	`5`
`HELIX`	`149 153`	`5`
`HELIX`	`158 178`	`21`
`STRAND`	`182 187`	`6`
`STRAND`	`191 194`	`4`
`HELIX`	`196 205`	`10`
`HELIX`	`208 211`	`4`
`STRAND`	`213 218`	`6`
`HELIX`	`225 239`	`15`
`STRAND`	`245 249`	`5`
`STRAND`	`274 276`	`3`
`STRAND`	`283 288`	`6`
`STRAND`	`297 301`	`5`
`HELIX`	`307 315`	`9`

Sequence information

Length: 441 AA [This is the length of the unprocessed precursor]

Molecular weight: 45844 Da [This is the MW of the unprocessed precursor]

CRC64: 87218E4537092AE5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPRPLRALL GAAAAALVSA AALAFPSQAA ANDSPFYVNP NMSSAEWVRN NPNDPRTPVI 

        70         80         90        100        110        120 
RDRIASVPQG TWFAHHNPGQ ITGQVDALMS AAQAAGKIPI LVVYNAPGRD CGNHSSGGAP 

       130        140        150        160        170        180 
SHSAYRSWID EFAAGLKNRP AYIIVEPDLI SLMSSCMQHV QQEVLETMAY AGKALKAGSS 

       190        200        210        220        230        240 
QARIYFDAGH SAWHSPAQMA SWLQQADISN SAHGIATNTS NYRWTADEVA YAKAVLSAIG 

       250        260        270        280        290        300 
NPSLRAVIDT SRNGNGPAGN EWCDPSGRAI GTPSTTNTGD PMIDAFLWIK LPGEADGCIA 

       310        320        330        340        350        360 
GAGQFVPQAA YEMAIAAGGT NPNPNPNPTP TPTPTPTPPP GSSGACTATY TIANEWNDGF 

       370        380        390        400        410        420 
QATVTVTANQ NITGWTVTWT FTDGQTITNA WNADVSTSGS SVTARNVGHN GTLSQGASTE 

       430        440 
FGFVGSKGNS NSVPTLTCAA S

P26222 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