You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002960_01033
You are here: Home > Sequence: MGYG000002960_01033
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 sp900555035 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900555035 | |||||||||||
| CAZyme ID | MGYG000002960_01033 | |||||||||||
| CAZy Family | CBM20 | |||||||||||
| CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 12503; End: 13939 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM20 | 136 | 219 | 3e-16 | 0.8888888888888888 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13419 | HAD_2 | 2.62e-44 | 271 | 450 | 1 | 178 | Haloacid dehalogenase-like hydrolase. |
| COG0546 | Gph | 5.76e-44 | 267 | 478 | 3 | 216 | Phosphoglycolate phosphatase, HAD superfamily [Energy production and conversion]. |
| PRK13222 | PRK13222 | 2.17e-42 | 272 | 456 | 10 | 198 | N-acetylmuramic acid 6-phosphate phosphatase MupP. |
| cd07512 | HAD_PGPase | 4.97e-41 | 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 | 2.13e-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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNT66032.1 | 1.13e-224 | 1 | 475 | 1 | 470 |
| ADE81398.1 | 5.63e-44 | 1 | 216 | 1 | 219 |
| QVJ80744.1 | 7.63e-44 | 1 | 216 | 1 | 219 |
| AGB29239.1 | 7.27e-42 | 1 | 256 | 1 | 233 |
| QVJ82132.1 | 1.12e-20 | 1 | 217 | 1 | 210 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2HI0_A | 8.34e-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 | 2.92e-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 | 3.62e-25 | 272 | 458 | 7 | 190 | X-raycrystal structure of a phosphoglycolate phosphatase from Aquifex aeolicus [Aquifex aeolicus] |
| 3MC1_A | 1.77e-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] |
Swiss-Prot Hits download full data without filtering help
| 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 | 1.60e-24 | 272 | 458 | 5 | 188 | Phosphoglycolate phosphatase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=gph PE=1 SV=1 |
| A4WW31 | 4.76e-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 |
| Q9S586 | 1.41e-20 | 272 | 472 | 17 | 215 | Phosphoglycolate phosphatase 1 OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=gph1 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 |
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 |
|---|---|---|---|---|---|
| 1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |