| IED ID | IndEnz0008000147 |
| Enzyme Type ID | cellulase000147 |
| Protein Name |
Mannan endo-1,4-beta-mannosidase A EC 3.2.1.78 Endo-beta-1,4-mannanase A Man5A |
| Gene Name | Pa_6_490 PODANS_6_490 |
| Organism | Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Podosporaceae Podospora Podospora anserina (Pleurage anserina) Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) |
| Enzyme Sequence | MKGLFAFGLGLLSLVNALPQAQGGGAAASAKVSGTRFVIDGKTGYFAGTNSYWIGFLTNNRDVDTTLDHIASSGLKILRVWGFNDVNNQPSGNTVWFQRLASSGSQINTGPNGLQRLDYLVRSAETRGIKLIIALVNYWDDFGGMKAYVNAFGGTKESWYTNARAQEQYKRYIQAVVSRYVNSPAIFAWELANEPRCKGCNTNVIFNWATQISDYIRSLDKDHLITLGDEGFGLPGQTTYPYQYGEGTDFVKNLQIKNLDFGTFHMYPGHWGVPTSFGPGWIKDHAAACRAAGKPCLLEEYGYESDRCNVQKGWQQASRELSRDGMSGDLFWQWGDQLSTGQTHNDGFTIYYGSSLATCLVTDHVRAINALPA |
| Enzyme Length | 373 |
| Uniprot Accession Number | B2B3C0 |
| Absorption | |
| Active Site | ACT_SITE 194; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:23558681; ACT_SITE 300; /note=Nucleophile; /evidence=ECO:0000305|PubMed:23558681 |
| Activity Regulation | |
| Binding Site | BINDING 81; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 193; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 230; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q99036; BINDING 267; /note=Substrate; /evidence=ECO:0000250|UniProtKB:B4XC07; BINDING 271; /note=Substrate; /evidence=ECO:0000250|UniProtKB:Q99036; BINDING 332; /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; Evidence={ECO:0000269|PubMed:21037302}; |
| DNA Binding | |
| EC Number | 3.2.1.78 |
| Enzyme Function | FUNCTION: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Hydrolyzes structurally different mannan polysaccharides, such as galactomannans, glucomannans, and beta-1,4-mannans from different sources, yielding principally mannobiose (PubMed:21037302). Also has transglycosylation activity (PubMed:23558681). {ECO:0000269|PubMed:21037302, ECO:0000269|PubMed:23558681}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:21037302}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.0. {ECO:0000269|PubMed:21037302}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (15); Binding site (6); Chain (1); Disulfide bond (3); Helix (15); Mutagenesis (2); Region (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Disulfide bond;Glycosidase;Hydrolase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q99036}. |
| Modified Residue | |
| Post Translational Modification | PTM: Not glycosylated. {ECO:0000269|PubMed:23558681}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3ZIZ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,183 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mg/ml for konjac glucomannan {ECO:0000269|PubMed:21037302}; KM=1.7 mg/ml for carob galactomannan {ECO:0000269|PubMed:21037302}; KM=4.7 mg/ml for locust bean gum galactomannan {ECO:0000269|PubMed:21037302}; KM=1.6 mg/ml for ivory nut mannan {ECO:0000269|PubMed:21037302}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |