Species | Alistipes sp902363575 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902363575 | |||||||||||
CAZyme ID | MGYG000000128_01279 | |||||||||||
CAZy Family | GH65 | |||||||||||
CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 569138; End: 572092 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH65 | 540 | 920 | 1.6e-143 | 0.9946236559139785 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK13807 | PRK13807 | 0.0 | 229 | 982 | 1 | 754 | maltose phosphorylase; Provisional |
COG1554 | ATH1 | 0.0 | 231 | 971 | 4 | 755 | Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism]. |
pfam03632 | Glyco_hydro_65m | 8.28e-166 | 540 | 923 | 1 | 387 | Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface. |
TIGR01990 | bPGM | 6.88e-76 | 6 | 190 | 3 | 185 | beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides] |
TIGR02009 | PGMB-YQAB-SF | 9.41e-65 | 2 | 189 | 1 | 185 | beta-phosphoglucomutase family hydrolase. This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBK62951.1 | 0.0 | 229 | 981 | 2 | 755 |
QKG79963.1 | 1.64e-312 | 232 | 976 | 4 | 759 |
QNR25625.1 | 1.18e-311 | 229 | 971 | 2 | 756 |
AFD07362.1 | 1.93e-308 | 231 | 977 | 3 | 759 |
QHL86664.1 | 2.13e-307 | 231 | 966 | 3 | 741 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1H54_A | 3.17e-216 | 231 | 980 | 3 | 754 | ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis] |
3WIQ_A | 2.09e-101 | 254 | 971 | 22 | 751 | Crystalstructure of kojibiose phosphorylase complexed with kojibiose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_A Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_B Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_C Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_D Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903] |
4KTP_A | 1.78e-67 | 237 | 961 | 13 | 734 | ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10] |
4KTR_A | 3.30e-67 | 237 | 961 | 13 | 734 | ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_C Chain C, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_D Chain D, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_E Chain E, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_F Chain F, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_G Chain G, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_H Chain H, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10] |
3NAS_A | 3.94e-46 | 6 | 216 | 6 | 216 | Thecrystal structure of beta-phosphoglucomutase from Bacillus subtilis [Bacillus subtilis],3NAS_B The crystal structure of beta-phosphoglucomutase from Bacillus subtilis [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O06993 | 1.99e-235 | 229 | 956 | 3 | 725 | Maltose phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=mdxK PE=3 SV=1 |
E6ENP7 | 5.46e-231 | 231 | 981 | 25 | 773 | Maltose phosphorylase OS=Enterococcus faecalis (strain TX4000 / JH2-2) OX=749493 GN=malP PE=1 SV=1 |
Q8L164 | 2.01e-125 | 236 | 967 | 13 | 759 | Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1 |
Q8RBL8 | 1.87e-99 | 238 | 958 | 16 | 751 | Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP PE=3 SV=1 |
Q8GRC3 | 6.07e-99 | 238 | 958 | 3 | 730 | Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000080 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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