[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=9438981 [NCBI, ExPASy, EBI, Israel, Japan] Hitomi J., Hatada Y., Kawaminami S., Kawai S., Ito S.; "Amino acid sequence and stereoselective hydrolytic reaction of an endo-1,4-beta-glucanase from a Bacillus strain."; Biosci. Biotechnol. Biochem. 61:2004-2009(1997).
[2]	PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-534. DOI=10.1016/0006-291X(90)90382-W; PubMed=2113383 [NCBI, ExPASy, EBI, Israel, Japan] Shoseyov O., Foong F., Hamamoto T., Doi R.H.; "Cloning of Clostridium cellulovorans endo-1,4-beta-glucanase genes."; Biochem. Biophys. Res. Commun. 169:667-672(1990).
[3]	SHOWS THAT SEQUENCE DID NOT ORIGINATE FROM C.CELLULOVORANS. Doi R.H.; Unpublished observations (JAN-2000).

Comments

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 9 (cellulase E) family.
SIMILARITY: Contains 1 CBM3 (carbohydrate binding type-3) domain.
CAUTION: Was originally (PubMed:2113383) thought to originate from Clostridium cellulovorans and was termed endoglucanase C (engC).

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

AB004098; BAA24918.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC5874; JC5874.

3D structure databases

HSSP

P26221; 1TF4. [HSSP ENTRY / PDB]

ModBase

P28622.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0030246;	Molecular function: carbohydrate binding (inferred from electronic annotation from InterPro).
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

IPR012341; 6hp_glycosidase.
IPR001956; CBD_3.
IPR001701; Glyco_hydro_9.
Graphical view of domain structure.

Gene3D

G3DSA:1.50.10.10; CelA/Cel48F_cat; 1.

PANTHER

PTHR22298:SF3; Glyco_hydro_9; 1.

Pfam

PF00942; CBM_3; 1.
PF00759; Glyco_hydro_9; 1.
Pfam graphical view of domain structure.

ProDom

PD001947; CBD_3; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS51172; CBM3; 1.
PS00592; GLYCOSYL_HYDROL_F9_1; 1.
PS00698; GLYCOSYL_HYDROL_F9_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`CHAIN`	`26 636`	`611`	`Endoglucanase 4.`	`PRO_0000007952`
`DOMAIN`	`478 635`	`158`	`CBM3.`
`ACT_SITE`	`400 400`		`By similarity.`
`ACT_SITE`	`438 438`		`By similarity.`
`ACT_SITE`	`447 447`		`By similarity.`
`CONFLICT`	`530 534`		`AKGFT -> CEGIH (in Ref. 2).`

Sequence information

Length: 636 AA [This is the length of the unprocessed precursor]

Molecular weight: 72245 Da [This is the MW of the unprocessed precursor]

CRC64: 76718BF57A8EF6A2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTRRWSFLVQ CFTFKKKEGV RSRYMSDYNY VEVLQKSILF YEAQRSGKLP ESNRLNWRGD 

        70         80         90        100        110        120 
SGLEDGKDVG HDLTGGWYDA GDHVKFGLPM AYSAAVLAWT VYEYREAYEE AELLDDMLDQ 

       130        140        150        160        170        180 
IKWATDYFLK AHTGPNEFWA QVGDGNADHG WWGPAEVMPM NRPAFKIDEH CPGTEVAAQT 

       190        200        210        220        230        240 
AAALAAGSII FKETDAPYAA KLLTHAKQLY AFADQYRGEY TDCVTNAQPF YNSWSGYIDE 

       250        260        270        280        290        300 
LIWGGIWLYL ATNDQTYLNK ALKAVEEWPK DWDYTFTMSW DNTFFLSQIL LARITKEKRF 

       310        320        330        340        350        360 
IESTERNLDY WSTGFVQNGK VERITYTPGG LAWLDQWGSL RYTANAAFLA FVYADWVSDQ 

       370        380        390        400        410        420 
EKKNRYQTFA IRQTHYMLGD NPQNRSYVVG FGKNPPMHPH HRTAHGSWSN QLTTPSSHRH 

       430        440        450        460        470        480 
TLYGPLVGGP NRQDQYTDDI SDYVSNEVAT DYNAAFTGNG AAVWSGQSKL PNFPPKEKVE 

       490        500        510        520        530        540 
DEFFVEAAVM SNDTTSTQIK AILYNRSGWP ARSSQSLSFR YYVNLSEIFA KGFTDKDIQV 

       550        560        570        580        590        600 
TAVYNEGASL SPLTVYDASS HIYFTEIDFT GVAIFPGGES LHKKEIQFRL SAPNGANIWD 

       610        620        630 
ASNDYSFQGL TSNMQKTARI PVFDQGDLVF GTLPNK

P28622 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