Detail Information for IndEnz0008000278
IED ID IndEnz0008000278
Enzyme Type ID cellulase000278
Protein Name Endoglucanase A
EC 3.2.1.4
Cellulase A
Endo-1,4-beta-glucanase A
Gene Name celA
Organism Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Caldicellulosiruptor Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Enzyme Sequence MVVTFLFILGVVYGVKPWQEARAGSFNYGEALQKAIMFYEFQMSGKLPNWVRNNWRGDSALKDGQDNGLDLTGGWFDAGDHVKFNLPMSYTGTMLSWAAYEYKDAFVKSGQLEHILNQIEWVNDYFVKCHPSKYVYYYQVGDGGKDHAWWGPAEVMQMERPSFKVTQSSPGSAVVAETAASLAAASIVLKDRNPTKAATYLQHAKDLYEFAEVTKSDSGYTAANGYYNSWSGFYDELSWAAVWLYLATNDSTYLTKAESYVQNWPKISGSNIIDYKWAHCWDDVHNGAALLLAKITDKDTYKQIIESHLDYWTTGYNGERIKYTPKGLAWLDQWGSLRYATTTAFLAFVYSDWSGCPTGKKETYRKFGESQIDYALGSTGRSFVVGFGTNPPKRPHHRTAHSSWADSQSIPSYHRHTLYGALVGGPGSDDSYTDDISNYVNNEVACDYNAGFVGALAKMYLLYGGNPIPDFKAIETPTNDEFFVEAGINASGTNFIEIKAIVNNQSGWPARATNKLKFRYFVDLSELIKAGYSPNQLTLSTNYNQGAKVSGPYVWDSSRNIYYILVDFTGTLIYPGGQDKYKKEVQFRIAAPQNVQWDNSNDYSFQDIKGVSSGSVVKTKYIPLYDEDIKVWGEEPGTSGVSPTPTASVTPTPTPTPTATPTPTPTPTVTPTPTVTATPTPTPTPTSTPTVTPTPTPVSTPATSGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGTTPAPTSTPTVTVTPTPTPTPTVTPTPTVTATPTPTPTPTSTPVSTPATGGQIKVLYANKETNSTTNTIRPWLKVVNSGSSSIDLSRVTIRYWYTVDGERAQSAISDWAQIGASNVTFKFVKLSSSVSGADYYLEIGFKSGAGQLQPGKDTGEIQIRFNKDDWSNYNQGNDWSWIQSMTSYGENEKVTAYIDGVLVWGQEPSGATPAPTVTPTPTVTPTPTPAPTPTATPTPTPTPTVTPTPTVAPTPTPSSTPSGLGKYGQRFMWLWNKIHDPASGYFNQDGIPYHSVETLICEAPDYGHLTTSEAFSYYVWLEAVYGKLTGDWSKFKTAWDTLEKYMIPSAEDQPMRSYDPNKPATYAGEWETPDKYPSPLEFNVPVGKDPLHNELVSTYGSTLMYGMHWLMDVDNWYGYGKRGDGVSRASFINTFQRGPEESVWETVPHPSWEEFKWGGPNGFLDLFIKDQNYSKQWRYTNAPDADARAIQATYWAKVWAKEQGKFNEISSYVGKAAKMGDYLRYAMFDKYFKPLGCQDKNAAGGTGYDSAHYLLSWYYAWGGALDGAWSWKIGCSHAHFGYQNPMAAWALANDSDMKPKSPNGASDWAKSLKRQIEFYRWLQSAEGAIAGGATNSWNGRYEKYPAGTATFYGMAYEPNPVYRDPGSNTWFGFQAWSMQRVAEYYYVTGDKDAGTLLEKWVSWIKSVVKLNSDGTFAIPSTLDWSGQPDTWNGTYTGNPNLHVKVVDYGTDLGITASLANALLYYSAGTKKYGVFDEEAKNLAKELLDRMWKLYRDEKGLSAPEKRADYKRFFEQEVYIPAGWTGKMPNGDVIKSGVKFIDIRSKYKQDPDWPKLEAAYKSGQVPEFRYHRFWAQCDIAIVNATYEILFGNQ
Enzyme Length 1742
Uniprot Accession Number P22534
Absorption
Active Site ACT_SITE 80; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU10140; ACT_SITE 396; /evidence=ECO:0000255|PROSITE-ProRule:PRU10059; ACT_SITE 434; /evidence=ECO:0000255|PROSITE-ProRule:PRU10060; ACT_SITE 443; /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 FUNCTION: The N-terminal domain of CelA codes for an endoglucanase activity on carboxymethylcellulose. The C-terminal domain probably acts synergistically to hydrolyze crystalline cellulose.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (4); Chain (1); Compositional bias (3); Domain (3); Region (8); Sequence conflict (1); Signal peptide (1)
Keywords Carbohydrate metabolism;Cellulose degradation;Glycosidase;Hydrolase;Polysaccharide degradation;Repeat;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification PTM: The linker region (also termed 'hinge') may be a potential site for proteolysis.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 193,697
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.2.1.4;