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CAZyme Information: MGYG000003912_00445
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Prevotella sp000435635 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp000435635 | |||||||||||
| CAZyme ID | MGYG000003912_00445 | |||||||||||
| CAZy Family | CBM20 | |||||||||||
| CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 135649; End: 137016 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM20 | 137 | 223 | 7.1e-16 | 0.9222222222222223 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG0546 | Gph | 2.36e-51 | 248 | 455 | 5 | 214 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]. |
| PRK13222 | PRK13222 | 1.34e-44 | 251 | 435 | 10 | 198 | N-acetylmuramic acid 6-phosphate phosphatase MupP. |
| cd02616 | HAD_PPase | 3.86e-44 | 247 | 455 | 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 | 6.35e-42 | 250 | 429 | 1 | 178 | Haloacid dehalogenase-like hydrolase. |
| cd07512 | HAD_PGPase | 1.52e-39 | 251 | 436 | 3 | 192 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNT66032.1 | 1.74e-174 | 1 | 455 | 1 | 471 |
| ADE81398.1 | 1.36e-44 | 1 | 214 | 1 | 218 |
| QVJ80744.1 | 2.51e-44 | 1 | 214 | 1 | 218 |
| AGB29239.1 | 8.44e-44 | 1 | 235 | 1 | 233 |
| QUT75082.1 | 3.77e-20 | 1 | 238 | 15 | 252 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2HI0_A | 1.67e-46 | 251 | 454 | 8 | 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 | 4.81e-26 | 251 | 433 | 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 | 5.97e-26 | 251 | 433 | 7 | 186 | X-raycrystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus [Aquifex aeolicus] |
| 3MC1_A | 8.73e-17 | 243 | 454 | 2 | 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 | 1.84e-15 | 252 | 433 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O67359 | 2.64e-25 | 251 | 433 | 5 | 184 | Phosphoglycolate phosphatase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=gph PE=1 SV=1 |
| Q9A5Z2 | 2.11e-23 | 246 | 450 | 8 | 215 | Phosphoglycolate phosphatase OS=Caulobacter vibrioides (strain ATCC 19089 / CB15) OX=190650 GN=gph PE=3 SV=1 |
| Q88QS2 | 6.48e-21 | 251 | 455 | 17 | 219 | Phosphoglycolate phosphatase OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=PP_0416 PE=3 SV=1 |
| Q9HZ62 | 6.66e-21 | 251 | 455 | 10 | 216 | N-acetylmuramic acid 6-phosphate phosphatase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=mupP PE=1 SV=1 |
| Q88A30 | 8.84e-21 | 251 | 455 | 17 | 226 | Phosphoglycolate phosphatase OS=Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) OX=223283 GN=PSPTO_0567 PE=3 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000037 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |