IED ID | IndEnz0008000387 |
Enzyme Type ID | cellulase000387 |
Protein Name |
Probable mannan endo-1,4-beta-mannosidase A EC 3.2.1.78 Endo-beta-1,4-mannanase A |
Gene Name | manA man1 An05g01320 |
Organism | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Enzyme Sequence | MKLSNALLTLASLALANVSTALPKASPAPSTSSSAASTSFASTSGLQFTIDGETGYFAGTNSYWIGFLTDNADVDLVMGHLKSSGLKILRVWGFNDVTSQPSSGTVWYQLHQDGKSTINTGADGLQRLDYVVSSAEQHDIKLIINFVNYWTDYGGMSAYVSAYGGSGETDFYTSDTMQSAYQTYIKTVVERYSNSSAVFAWELANEPRCPSCDTSVLYNWIEKTSKFIKGLDADRMVCIGDEGFGLNIDSDGSYPYQFSEGLNFTMNLGIDTIDFGTLHLYPDSWGTSDDWGNGWITAHGAACKAAGKPCLLEEYGVTSNHCSVEGSWQKTALSTTGVGADLFWQYGDDLSTGKSPDDGNTIYYGTSDYQCLVTDHVAAIGSA |
Enzyme Length | 383 |
Uniprot Accession Number | A2QKT4 |
Absorption | |
Active Site | ACT_SITE 206; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:Q99036; ACT_SITE 314; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q99036 |
Activity Regulation | |
Binding Site | BINDING 92; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 205; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 281; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 344; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; |
DNA Binding | |
EC Number | 3.2.1.78 |
Enzyme Function | FUNCTION: Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (15); Binding site (4); Chain (1); Glycosylation (3); Helix (14); Signal peptide (1); Turn (2) |
Keywords | 3D-structure;Carbohydrate metabolism;Glycoprotein;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3WH9; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 41,247 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.2.1.78; |