| IED ID | IndEnz0004000268 |
| Enzyme Type ID | xylanase000268 |
| Protein Name |
Beta-galactosidase BgaA Beta-gal EC 3.2.1.23 Alpha-L-arabinopyranosidase |
| Gene Name | bgaA Clocel_2022 |
| Organism | Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium cellulovorans Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) |
| Enzyme Sequence | MRIGVDYYPEHWDRQLWEKDAQLMKEIGVKVVRLAEFAWCKLEPIEGQYDFKWLDDVIEIFSVRNIEIVLGTPTNTPPLWLYEKYPDAIQVNESGERQFIGIRGHRCYNSSSMRKYTKAIVEAMTERYANNKAVIGWQIDNELDATHCCCDNCTEKFRGWLKNKYSTLENINKEYGNVVWSGEYSAWSQVTAPLGGSPFLNPSYLLDYNRFASDSMVEYIDFQREIIRKNCPSQFITTNTWFTGNLPNFYDAFENLDFVSYDNYPTTNEITDEEELHSHAFHCDLMRGIKKKNFWIMEQLSGTPGCWMPMQRTPKPGMIKGYSFQAIGRGAETVVHFRWRNAIIGAEMFWHGILDHSNVKGRRFYEFAELCREVNKINEEIPDYKINNEVAILYSSDQDFAFKIQPQVEGLYYLQQLKAFHNALIRLGVGTDIINWSESLNKYKVVIAPTLYLTDDNVTTELYRFVEAGGTLILTNRTGVKNMNNVCLMEQMPSNLKECAGVVVKEYDPIGHSIHTIKDEAGKVYQCKQWCDILEPTTAKVIATYNDDFYIDEAAVTVNKYKKGNVYYLGTVFNSDYYIELLSKILDEKELPYYKKLPYGLELSVLENENGKYLMVFNNSNEIKCFEGKHEGKSIIRNELDGKSFTLEPYGIEVLQLVE |
| Enzyme Length | 659 |
| Uniprot Accession Number | D9SM34 |
| Absorption | |
| Active Site | ACT_SITE 142; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:O69315; ACT_SITE 298; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O69315 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by Cu(2+), Hg(2+) and Zn(2+). No effect with Ca(2+), Mg(2+), Mn(2+) or excess EDTA (10 mM). {ECO:0000269|PubMed:12446636}. |
| Binding Site | BINDING 103; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O69315; BINDING 141; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O69315; BINDING 307; /note=Substrate; /evidence=ECO:0000250|UniProtKB:O69315 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:12446636}; |
| DNA Binding | |
| EC Number | 3.2.1.23 |
| Enzyme Function | FUNCTION: Involved in plant cell wall degradation in cooperation with cellulosome. Hydrolyzes both p-nitrophenyl-alpha-L-arabinopyranoside (pNPAp) and p-nitrophenyl-beta-D-galactopyranoside (pNPGp), with higher activity for pNPAp. Shows hydrolysis activity against p-nitrophenyl-beta-D-fucopyranoside (pNPFp), but not against p-nitrophenyl-alpha-L-arabinofuranoside (pNPAf), o-nitrophenyl-beta-D-galactopyranoside (oNPGp), p-nitrophenyl-beta-D-xylopyranoside (pNPXp), p-nitrophenyl-beta-D-glucopyranoside (pNPGLp), p-nitrophenyl-beta-D-cellobiopyranoside (pNPCp), p-nitrophenyl-beta-lactopyranoside (pNPLp) or p-nitrophenyl-alpha-galactopyranoside (pNPalphaGp). No detectable activity against arabinan or arabinoxylan, but activity against arabinogalactan can be detected. Increases degradation activity of alpha-L-arabinofuranosidase (ArfA) and endo-1,4-beta-xylanase (XynA) when corn fiber gum and corn stem powder are used as substrates. {ECO:0000269|PubMed:12446636}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius for activities against both pNPAp and pNPGp when incubated 10 minutes at pH 6.0. Both activities completely lost after heating at 50 degrees Celsius for 20 minutes. {ECO:0000269|PubMed:12446636}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for activities against both pNPAp and pNPGp. Stable in the range of pH 6.0-8.0. {ECO:0000269|PubMed:12446636}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (3); Chain (1); Metal binding (4) |
| Keywords | Direct protein sequencing;Glycosidase;Hydrolase;Metal-binding;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 76,464 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.51 mM for pNPAp (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; KM=6.06 mM for pNPGp (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; Vmax=10.4 umol/min/mg enzyme with pNPAp as substrate (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; Vmax=2.5 umol/min/mg enzyme with pNPGp as substrate (at 37 degrees Celsius and pH 6.0) {ECO:0000269|PubMed:12446636}; |
| Metal Binding | METAL 107; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O69315; METAL 148; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O69315; METAL 150; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O69315; METAL 153; /note=Zinc; /evidence=ECO:0000250|UniProtKB:O69315 |
| Rhea ID | |
| Cross Reference Brenda |