Species | Prevotella sp900767615 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900767615 | |||||||||||
CAZyme ID | MGYG000002603_00258 | |||||||||||
CAZy Family | CBM20 | |||||||||||
CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 25361; End: 26797 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM20 | 136 | 219 | 4.4e-16 | 0.8888888888888888 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13419 | HAD_2 | 2.04e-43 | 271 | 450 | 1 | 178 | Haloacid dehalogenase-like hydrolase. |
COG0546 | Gph | 1.90e-42 | 267 | 478 | 3 | 216 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]. |
PRK13222 | PRK13222 | 3.15e-42 | 272 | 456 | 10 | 198 | N-acetylmuramic acid 6-phosphate phosphatase MupP. |
cd07512 | HAD_PGPase | 1.05e-40 | 272 | 476 | 3 | 214 | 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. |
cd02616 | HAD_PPase | 6.81e-39 | 268 | 475 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNT66032.1 | 5.61e-225 | 1 | 475 | 1 | 470 |
ADE81398.1 | 2.63e-45 | 1 | 264 | 1 | 253 |
QVJ80744.1 | 6.60e-45 | 1 | 264 | 1 | 253 |
AGB29239.1 | 1.04e-40 | 1 | 276 | 1 | 254 |
QVJ82132.1 | 6.24e-19 | 1 | 217 | 1 | 210 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2HI0_A | 3.07e-42 | 268 | 475 | 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 | 4.01e-25 | 272 | 458 | 5 | 188 | 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 | 4.96e-25 | 272 | 458 | 7 | 190 | X-raycrystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus [Aquifex aeolicus] |
3MC1_A | 6.08e-18 | 268 | 475 | 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] |
2HSZ_A | 9.17e-15 | 273 | 455 | 28 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O33512 | 1.45e-25 | 272 | 477 | 6 | 215 | Phosphoglycolate phosphatase OS=Rhodobacter capsulatus OX=1061 GN=cbbZ PE=3 SV=1 |
O67359 | 2.20e-24 | 272 | 458 | 5 | 188 | Phosphoglycolate phosphatase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=gph PE=1 SV=1 |
A4WW31 | 6.51e-21 | 272 | 455 | 5 | 190 | Phosphoglycolate phosphatase OS=Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) OX=349102 GN=cbbZ PE=3 SV=1 |
Q98ML8 | 3.76e-20 | 272 | 456 | 7 | 195 | Phosphoglycolate phosphatase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=gph PE=3 SV=1 |
Q9A5Z2 | 6.31e-20 | 260 | 456 | 1 | 201 | Phosphoglycolate phosphatase OS=Caulobacter vibrioides (strain ATCC 19089 / CB15) OX=190650 GN=gph PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.