| IED ID | IndEnz0008000174 |
| Enzyme Type ID | cellulase000174 |
| Protein Name |
Mannan endo-1,4-beta-mannosidase EC 3.2.1.78 Beta-mannanase Mannanase 26A Man26A Mannanase A ManA |
| Gene Name | BAD_1030 |
| Organism | Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Bifidobacteriales Bifidobacteriaceae Bifidobacterium Bifidobacterium adolescentis Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) |
| Enzyme Sequence | MKTTVTKLLATVAAASTIFGMSTLPAFAAEGKSASNGNSVNISDVNATAETRALFDKLKNSGKGDLRFGQQHATDENISSSASQGDVYETTGKYPAVFGWDAGLALRGAEKPGSGADKNANAKALAQNITDADSKGAIVTLSAHWCNPGTGKDFNDTTAVASELLPGGKYSGTFNKELDAIAATAQRAKRSDGTLIPIIFRPLHENNGSWFWWGATHASASEYKELYRYIVDYLRDVKDVHNLLYAYSPGGVFNGDSTDYLATYPGDQWVDVLGYDEYDSDDSADDSSAWINTVVKDMKMVSDQASQRGKIVALTEFGRSGDRKFKESGTGDKDTKFFSELAEALAENVPSTAYMMTWANFGGGGDNFQAYTSWKGSDGEADFKAFADSNKNLMASKDNVDYSNAPAAAMQNGSARIVTPVDGNRVTDTKVVVRVKTEGVKYSDLDLNSAIVTTDRGQNVKLKYSCNGYFTGILDLNAAGINLDQSKLTLTPQVKTKDGKTLAAADGNGSVTVKLGAKPEQTVDNVEDFDSYDNEAELQSVYSPSHSTKSNLTLVDSPEDNGTKAGNIHYDFVSYPEYNGFQRSHTPKQDWSGFSKLNMFLKADGSDHKFVVQVNAGGVTFEAYPKIDGTDGHVVSLNFGDADGNGGDFAPASWDTAHAGMKLSQKLLSKVGSFALYINDNGGNRPKSGDLTLDSIKLDGKRDAYAPNTNPTPGNTAKAQSVDDFSGYSDDAAAQSAWGNRGHTEVLSLDEGPTDGSKALRFKYDFSNGGWYDVAKYLDGANWSGESVLAFQVKGDGSGNAIGLQIGTSDGKYFLASVKLDFTGWKQIEIPLVDNANLTQSWPEDANKDNPMTEDDLASIKELVFASQQWNSESDGLDSSIADIKVEPAENTSNEQTPKDESKTEVKADKEQEQSEDTSADVTAQDPATCPISDEDSKGSTGNTTVTVKPTPDTKEPADNTGKDGLSRTGSNIISAIAAVAVLLLGGCAVLIARKRKGGDIE |
| Enzyme Length | 1002 |
| Uniprot Accession Number | A1A278 |
| Absorption | |
| Active Site | ACT_SITE 205; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P49424; ACT_SITE 316; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P49424 |
| Activity Regulation | |
| Binding Site | BINDING 144; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P49424; BINDING 210; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P49424; BINDING 278; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P49424; BINDING 384; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P49424 |
| 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:23064345}; |
| DNA Binding | |
| EC Number | 3.2.1.78 |
| Enzyme Function | FUNCTION: Beta-mannanase likely involved in the utilization of carbohydrates in the human gut. Catalyzes the hydrolysis of different beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan, as well as carob and guar gum galactomannans, to a mixture of oligosaccharides. The dominant product from ivory nut mannan is found to be mannotriose; mannobiose and mannotetraose are produced to a lesser extent. Does not hydrolyze mannobiose, and hydrolyzes mannotriose at a significantly lower rate than the longer oligosaccharides. {ECO:0000269|PubMed:23064345}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. Retains over 90% of its activity in the pH range of 5 to 6. {ECO:0000269|PubMed:23064345}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (4); Chain (1); Compositional bias (3); Domain (3); Modified residue (1); Motif (1); Propeptide (1); Region (2); Signal peptide (1); Site (1) |
| Keywords | Carbohydrate metabolism;Cell wall;Glycosidase;Hydrolase;Peptidoglycan-anchor;Polysaccharide degradation;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-anchor {ECO:0000305}. Note=Is likely to be cell attached, either by the sortase mechanism (LPXTG motif) or via a C-terminal transmembrane helix. {ECO:0000269|PubMed:23064345}. |
| Modified Residue | MOD_RES 969; /note=Pentaglycyl murein peptidoglycan amidated threonine; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 966..970; /note=LPXTG sorting signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00477 |
| Gene Encoded By | |
| Mass | 106,997 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |