Detail Information for IndEnz0008000387
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;