Species | Prevotella sp900556795 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556795 | |||||||||||
CAZyme ID | MGYG000004456_00734 | |||||||||||
CAZy Family | CBM20 | |||||||||||
CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 109691; End: 111073 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM20 | 138 | 220 | 3e-16 | 0.8777777777777778 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0546 | Gph | 3.17e-45 | 248 | 460 | 3 | 214 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]. |
cd07512 | HAD_PGPase | 2.57e-44 | 253 | 459 | 3 | 213 | 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. |
PRK13222 | PRK13222 | 8.26e-44 | 253 | 457 | 10 | 208 | N-acetylmuramic acid 6-phosphate phosphatase MupP. |
cd02616 | HAD_PPase | 3.22e-38 | 249 | 460 | 1 | 205 | 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. |
pfam13419 | HAD_2 | 4.09e-36 | 252 | 434 | 1 | 178 | Haloacid dehalogenase-like hydrolase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT66032.1 | 1.01e-201 | 1 | 460 | 1 | 471 |
QVJ80744.1 | 9.07e-53 | 1 | 241 | 1 | 249 |
ADE81398.1 | 1.70e-52 | 1 | 240 | 1 | 248 |
AGB29239.1 | 7.24e-42 | 1 | 237 | 1 | 233 |
QVJ82132.1 | 8.73e-24 | 1 | 230 | 1 | 222 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2HI0_A | 2.60e-46 | 249 | 459 | 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 | 1.04e-22 | 253 | 460 | 5 | 203 | 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 | 1.28e-22 | 253 | 460 | 7 | 205 | X-raycrystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus [Aquifex aeolicus] |
2HSZ_A | 1.93e-17 | 249 | 439 | 23 | 218 | 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 | 4.76e-15 | 253 | 459 | 8 | 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 |
---|---|---|---|---|---|---|
Q98ML8 | 2.21e-22 | 253 | 440 | 7 | 195 | Phosphoglycolate phosphatase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=gph PE=3 SV=1 |
Q9A5Z2 | 5.16e-22 | 251 | 440 | 11 | 201 | Phosphoglycolate phosphatase OS=Caulobacter vibrioides (strain ATCC 19089 / CB15) OX=190650 GN=gph PE=3 SV=1 |
O67359 | 5.72e-22 | 253 | 460 | 5 | 203 | Phosphoglycolate phosphatase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=gph PE=1 SV=1 |
Q4FPT7 | 6.09e-22 | 248 | 439 | 2 | 198 | Phosphoglycolate phosphatase OS=Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4) OX=259536 GN=Psyc_2124 PE=3 SV=1 |
Q8UEY9 | 2.05e-20 | 253 | 440 | 11 | 199 | 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 |
---|---|---|---|---|---|
1.000072 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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