Detail Information for IndEnz0008000218
IED ID IndEnz0008000218
Enzyme Type ID cellulase000218
Protein Name Endoglucanase 4
EC 3.2.1.4
Cellulase 4
EG-IV
Endo-1,4-beta-glucanase 4
Gene Name
Organism Bacillus sp. (strain KSM-522)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus unclassified Bacillus (in: Bacteria) Bacillus sp. (strain KSM-522)
Enzyme Sequence MTRRWSFLVQCFTFKKKEGVRSRYMSDYNYVEVLQKSILFYEAQRSGKLPESNRLNWRGDSGLEDGKDVGHDLTGGWYDAGDHVKFGLPMAYSAAVLAWTVYEYREAYEEAELLDDMLDQIKWATDYFLKAHTGPNEFWAQVGDGNADHGWWGPAEVMPMNRPAFKIDEHCPGTEVAAQTAAALAAGSIIFKETDAPYAAKLLTHAKQLYAFADQYRGEYTDCVTNAQPFYNSWSGYIDELIWGGIWLYLATNDQTYLNKALKAVEEWPKDWDYTFTMSWDNTFFLSQILLARITKEKRFIESTERNLDYWSTGFVQNGKVERITYTPGGLAWLDQWGSLRYTANAAFLAFVYADWVSDQEKKNRYQTFAIRQTHYMLGDNPQNRSYVVGFGKNPPMHPHHRTAHGSWSNQLTTPSSHRHTLYGPLVGGPNRQDQYTDDISDYVSNEVATDYNAAFTGNGAAVWSGQSKLPNFPPKEKVEDEFFVEAAVMSNDTTSTQIKAILYNRSGWPARSSQSLSFRYYVNLSEIFAKGFTDKDIQVTAVYNEGASLSPLTVYDASSHIYFTEIDFTGVAIFPGGESLHKKEIQFRLSAPNGANIWDASNDYSFQGLTSNMQKTARIPVFDQGDLVFGTLPNK
Enzyme Length 636
Uniprot Accession Number P28622
Absorption
Active Site ACT_SITE 82; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 400; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 438; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 447; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
DNA Binding
EC Number 3.2.1.4
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (4); Chain (1); Domain (1); Sequence conflict (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 72,245
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda