Species | Eisenbergiella sp900544445 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900544445 | |||||||||||
CAZyme ID | MGYG000003063_00913 | |||||||||||
CAZy Family | GH105 | |||||||||||
CAZyme Description | Phosphoglycolate phosphatase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 27280; End: 28905 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH105 | 222 | 539 | 4e-100 | 0.9759036144578314 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4225 | YesR | 1.15e-111 | 204 | 538 | 12 | 348 | Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism]. |
pfam07470 | Glyco_hydro_88 | 1.62e-99 | 208 | 538 | 9 | 338 | Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases. |
cd04305 | HAD_Neu5Ac-Pase_like | 9.46e-14 | 37 | 138 | 11 | 108 | human N-acetylneuraminate-9-phosphate phosphatase, Escherichia coli house-cleaning phosphatase YjjG, and related phosphatases. N-acetylneuraminate-9- phosphatase (Neu5Ac-9-Pase; E.C. 3.1.3.29) catalyzes the dephosphorylation of N-acylneuraminate 9-phosphate during the synthesis of N-acetylneuraminate; Escherichia coli nucleotide phosphatase YjjG has a broad pyrimidine nucleotide activity spectrum and functions as an in vivo house-cleaning phosphatase for noncanonical pyrimidine nucleotides. 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. |
COG1011 | YigB | 2.51e-13 | 17 | 161 | 78 | 218 | FMN phosphatase YigB, HAD superfamily [Coenzyme transport and metabolism]. |
cd02588 | HAD_L2-DEX | 1.18e-12 | 39 | 159 | 95 | 208 | L-2-haloacid dehalogenase. L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloacids to produce the corresponding D-2-hydroxyacids with an inversion of the C2-configuration. 2-haloacid dehalogenases are of interest for their potential to degrade recalcitrant halogenated environmental pollutants and their use in the synthesis of industrial chemicals. 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 |
---|---|---|---|---|---|
QEH70918.1 | 2.00e-153 | 188 | 539 | 8 | 358 |
QQR00386.1 | 1.79e-152 | 188 | 538 | 10 | 359 |
ANU44854.1 | 1.79e-152 | 188 | 538 | 10 | 359 |
BCJ96760.1 | 9.17e-150 | 187 | 538 | 10 | 360 |
SET92327.1 | 2.89e-149 | 183 | 538 | 1 | 355 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3PMM_A | 3.70e-96 | 226 | 538 | 63 | 376 | ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578] |
3QWT_A | 7.93e-95 | 226 | 538 | 62 | 375 | ChainA, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_B Chain B, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_C Chain C, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_D Chain D, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A] |
4XUV_A | 2.16e-85 | 185 | 538 | 7 | 367 | Crystalstructure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126],4XUV_B Crystal structure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126] |
1NC5_A | 1.10e-26 | 221 | 510 | 31 | 336 | Structureof Protein of Unknown Function of YteR from Bacillus Subtilis [Bacillus subtilis],2D8L_A Crystal Structure of Unsaturated Rhamnogalacturonyl Hydrolase in complex with dGlcA-GalNAc [Bacillus subtilis] |
2GH4_A | 4.35e-26 | 221 | 510 | 21 | 326 | ChainA, Putative glycosyl hydrolase yteR [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O31521 | 1.03e-56 | 229 | 539 | 29 | 335 | Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1 |
O34559 | 6.00e-26 | 221 | 510 | 31 | 336 | Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1 |
P9WF04 | 1.43e-14 | 231 | 505 | 92 | 380 | Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_28 PE=1 SV=1 |
P0A8Y1 | 9.51e-10 | 54 | 169 | 113 | 222 | Pyrimidine 5'-nucleotidase YjjG OS=Escherichia coli (strain K12) OX=83333 GN=yjjG PE=1 SV=1 |
P0A8Y2 | 9.51e-10 | 54 | 169 | 113 | 222 | Pyrimidine 5'-nucleotidase YjjG OS=Escherichia coli O157:H7 OX=83334 GN=yjjG PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000039 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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