IED ID | IndEnz0008000290 |
Enzyme Type ID | cellulase000290 |
Protein Name |
Major extracellular endoglucanase EC 3.2.1.4 Cellulase Endo-1,4-beta-glucanase |
Gene Name | engXCA XCC3521 |
Organism | Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas Xanthomonas campestris Xanthomonas campestris pv. campestris Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) |
Enzyme Sequence | MSIFRTASTLALATALALAAGPAFSYSINNSRQIVDDSGKVVQLKGVNVFGFETGNHVMHGLWARNWKDMIVQMQGLGFNAVRLPFCPATLRSDTMPASIDYSRNADLQGLTSLQILDKVIAEFNARGMYVLLDHHTPDCAGISELWYTGSYTEAQWLADLRFVANRYKNVPYVLGLDLKNEPHGAATWGTGNAATDWNKAAERGSAAVLAVAPKWLIAVEGITDNPVCSTNGGIFWGGNLQPLACTPLNIPANRLLLAPHVYGPDVFVQSYFNDSNFPNNMPAIWERHFGQFAGTHALLLGEFGGKYGEGDARDKTWQDALVKYLRSKGINQGFYWSWNPNSGDTGGILRDDWTSVRQDKMTLLRTLWGTAGNTTPTPTPTPTPTPTPTPTPTPTPTPGTSTFSTKVIVDNSWNGGYCNRVQVTNTGTASGTWSIAVPVTGTVNNAWNATWSQSGSTLRASGVDFNRTLAAGATAEFGFCAAS |
Enzyme Length | 484 |
Uniprot Accession Number | P19487 |
Absorption | |
Active Site | ACT_SITE 182; /note=Proton donor; /evidence=ECO:0000250; ACT_SITE 303; /note=Nucleophile; /evidence=ECO:0000250 |
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 (2); Beta strand (14); Chain (1); Compositional bias (1); Domain (1); Helix (12); Region (2); Sequence conflict (1); Signal peptide (1); Turn (8) |
Keywords | 3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Glycosidase;Hydrolase;Polysaccharide degradation;Reference proteome;Repeat;Signal |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000269|PubMed:2373365 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4TUF; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 52,242 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.4; |