Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
CAZyme ID | MGYG000004495_00312 | |||||||||||
CAZy Family | CBM20 | |||||||||||
CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6312; End: 7778 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM20 | 141 | 224 | 1.2e-18 | 0.8888888888888888 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0546 | Gph | 3.99e-47 | 278 | 487 | 1 | 213 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]. |
PRK13222 | PRK13222 | 5.68e-42 | 285 | 467 | 10 | 197 | N-acetylmuramic acid 6-phosphate phosphatase MupP. |
cd02616 | HAD_PPase | 2.90e-41 | 281 | 487 | 1 | 204 | pyrophosphatase similar to Bacillus subtilis PpaX. This family includes Bacillus subtilis PpaX which hydrolyzes pyrophosphate formed during serine-46-phosphorylated HPr (P-Ser-HPr) dephosphorylation by the bifunctional enzyme HPr kinase/phosphorylase. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. |
cd07512 | HAD_PGPase | 3.00e-39 | 285 | 467 | 3 | 190 | haloacid dehalogenase-like superfamily phosphoglycolate phosphatase, similar to Rhodobacter sphaeroides CbbZ. Phosphoglycolate phosphatase catalyzes the dephosphorylation of phosphoglycolate; its activity requires divalent cations, especially Mg++. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. |
pfam13419 | HAD_2 | 8.70e-38 | 284 | 462 | 1 | 178 | Haloacid dehalogenase-like hydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT66032.1 | 3.47e-155 | 1 | 487 | 1 | 470 |
ADE81398.1 | 1.77e-55 | 1 | 249 | 1 | 253 |
QVJ80744.1 | 2.42e-55 | 1 | 249 | 1 | 253 |
AGB29239.1 | 1.37e-47 | 1 | 235 | 1 | 227 |
QUT75082.1 | 5.01e-26 | 1 | 237 | 15 | 244 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2HI0_A | 7.36e-40 | 281 | 487 | 4 | 233 | Crystalstructure of putative phosphoglycolate phosphatase (YP_619066.1) from Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 at 1.51 A resolution [Lactobacillus delbrueckii],2HI0_B Crystal structure of putative phosphoglycolate phosphatase (YP_619066.1) from Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 at 1.51 A resolution [Lactobacillus delbrueckii] |
2YY6_A | 2.11e-24 | 285 | 466 | 5 | 184 | CrystalStructure of the phosphoglycolate phosphatase from Aquifex aeolicus VF5 [Aquifex aeolicus VF5],2YY6_B Crystal Structure of the phosphoglycolate phosphatase from Aquifex aeolicus VF5 [Aquifex aeolicus VF5] |
2NYV_A | 2.60e-24 | 285 | 466 | 7 | 186 | X-raycrystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus [Aquifex aeolicus] |
2HSZ_A | 5.18e-15 | 286 | 466 | 28 | 217 | Crystalstructure of a predicted phosphoglycolate phosphatase (hs_0176) from haemophilus somnus 129pt at 1.90 A resolution [Histophilus somni 129PT],2HSZ_B Crystal structure of a predicted phosphoglycolate phosphatase (hs_0176) from haemophilus somnus 129pt at 1.90 A resolution [Histophilus somni 129PT] |
3MC1_A | 1.77e-14 | 281 | 487 | 4 | 210 | Crystalstructure of a predicted phosphatase from Clostridium acetobutylicum [Clostridium acetobutylicum],3MC1_B Crystal structure of a predicted phosphatase from Clostridium acetobutylicum [Clostridium acetobutylicum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O67359 | 1.15e-23 | 285 | 466 | 5 | 184 | Phosphoglycolate phosphatase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=gph PE=1 SV=1 |
Q88QS2 | 3.20e-21 | 285 | 484 | 17 | 215 | Phosphoglycolate phosphatase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=PP_0416 PE=3 SV=1 |
Q98ML8 | 6.15e-21 | 285 | 487 | 7 | 221 | Phosphoglycolate phosphatase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=gph PE=3 SV=1 |
Q3K5U8 | 2.04e-20 | 285 | 484 | 17 | 215 | Phosphoglycolate phosphatase OS=Pseudomonas fluorescens (strain Pf0-1) OX=205922 GN=Pfl01_5119 PE=3 SV=1 |
Q8UEY9 | 2.42e-20 | 285 | 466 | 11 | 197 | Phosphoglycolate phosphatase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=gph PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000059 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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