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CAZyme Information: MGYG000001436_03018

You are here: Home > Sequence: MGYG000001436_03018

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 Paenibacillus_F sp000411255
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_F; Paenibacillus_F sp000411255
CAZyme ID MGYG000001436_03018
CAZy Family CBM9
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1869 201024.9 5.3215
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001436 6290841 Isolate not provided not provided
Gene Location Start: 132040;  End: 137649  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001436_03018.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM9 93 280 1.9e-28 0.9945054945054945

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08563 GDPD_TtGDE_like 5.57e-50 1097 1330 1 229
Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE.
cd08582 GDPD_like_2 6.16e-45 1099 1333 1 233
Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial glycerophosphodiester phosphodiesterases. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized bacterial glycerophosphodiester phosphodiesterase and similar proteins. They show high sequence similarity to Escherichia coli glycerophosphodiester phosphodiesterase, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.
COG0584 UgpQ 5.03e-42 1094 1330 3 246
Glycerophosphoryl diester phosphodiesterase [Lipid transport and metabolism].
cd08601 GDPD_SaGlpQ_like 2.78e-40 1099 1331 3 248
Glycerophosphodiester phosphodiesterase domain of Staphylococcus aureus and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized glycerophosphodiester phosphodiesterase (GP-GDE, EC 3.1.4.46) from Staphylococcus aureus, Bacillus subtilis and similar proteins. Members in this family show very high sequence similarity to Escherichia coli periplasmic phosphodiesterase GlpQ, which catalyzes the Ca2+-dependent degradation of periplasmic glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols.
cd08556 GDPD 7.11e-40 1099 1330 1 189
Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins. The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QAV16877.1 0.0 43 1869 1 1808
QJD84974.1 0.0 43 1869 1 1815
CQR54490.1 0.0 79 1869 81 1950
QQZ58765.1 0.0 83 1869 85 1944
AWB43051.1 0.0 43 1869 1 1838

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2PZ0_A 2.14e-35 1096 1329 11 239
ChainA, Glycerophosphoryl diester phosphodiesterase [Caldanaerobacter subterraneus subsp. tengcongensis MB4],2PZ0_B Chain B, Glycerophosphoryl diester phosphodiesterase [Caldanaerobacter subterraneus subsp. tengcongensis MB4]
5T91_A 4.76e-26 1100 1330 16 257
Crystalstructure of B. subtilis 168 GlpQ in complex with bicine [Bacillus subtilis subsp. subtilis str. 168],5T9B_G Crystal structure of B. subtilis 168 GlpQ in complex with glycerol-3-phosphate (5 minute soak) [Bacillus subtilis subsp. subtilis str. 168],5T9C_E Crystal structure of B. subtilis 168 GlpQ in complex with glycerol-3-phosphate (1 hour soak) [Bacillus subtilis subsp. subtilis str. 168]
4R7O_A 1.49e-25 1100 1330 19 281
CrystalStructure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_B Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_C Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_D Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_E Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_F Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames],4R7O_G Crystal Structure of Putative Glycerophosphoryl Diester Phosphodiesterasefrom Bacillus anthraci [Bacillus anthracis str. Ames]
2OOG_A 4.24e-23 1100 1331 27 271
ChainA, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2OOG_B Chain B, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2OOG_C Chain C, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2OOG_D Chain D, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2OOG_E Chain E, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2OOG_F Chain F, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_A Chain A, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_B Chain B, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_C Chain C, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_D Chain D, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_E Chain E, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_F Chain F, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_G Chain G, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315],2P76_H Chain H, Glycerophosphoryl diester phosphodiesterase [Staphylococcus aureus subsp. aureus N315]
4OEC_A 1.40e-18 1099 1254 9 153
Crystalstructure of glycerophosphodiester phosphodiesterase from Thermococcus kodakarensis KOD1 [Thermococcus kodakarensis KOD1],4OEC_B Crystal structure of glycerophosphodiester phosphodiesterase from Thermococcus kodakarensis KOD1 [Thermococcus kodakarensis KOD1],4OEC_C Crystal structure of glycerophosphodiester phosphodiesterase from Thermococcus kodakarensis KOD1 [Thermococcus kodakarensis KOD1],4OEC_D Crystal structure of glycerophosphodiester phosphodiesterase from Thermococcus kodakarensis KOD1 [Thermococcus kodakarensis KOD1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O07592 4.26e-28 1098 1330 2 230
Putative glycerophosphodiester phosphodiesterase YhdW OS=Bacillus subtilis (strain 168) OX=224308 GN=yhdW PE=3 SV=1
P37965 4.56e-25 1100 1330 41 282
Glycerophosphodiester phosphodiesterase OS=Bacillus subtilis (strain 168) OX=224308 GN=glpQ PE=1 SV=1
P54527 1.20e-22 1099 1330 4 232
Uncharacterized protein YqiK OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiK PE=4 SV=2
P38536 8.24e-21 1662 1868 1662 1861
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535 2.47e-18 1656 1858 887 1077
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX 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
0.875206 0.063907 0.059717 0.000257 0.000168 0.000727

TMHMM  Annotations      download full data without filtering help

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49 71