You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002369_02435
You are here: Home > Sequence: MGYG000002369_02435
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 | Clostridioides difficile | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Clostridioides; Clostridioides difficile | |||||||||||
| CAZyme ID | MGYG000002369_02435 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | Mannosylglucosyl-3-phosphoglycerate phosphatase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 2657900; End: 2659741 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd07408 | MPP_SA0022_N | 7.62e-130 | 32 | 283 | 1 | 255 | Staphylococcus aureus SA0022 and related proteins, N-terminal metallophosphatase domain. SA0022 is an uncharacterized Staphylococcus aureus UshA-like protein with two putative domains, an N-terminal metallophosphatase domain and a C-terminal nucleotidase domain. SA0022 also contains a putative C-terminal cell wall anchor domain. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. |
| COG0737 | UshA | 7.59e-97 | 31 | 500 | 26 | 504 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09419 | PRK09419 | 2.47e-94 | 31 | 505 | 660 | 1143 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| PRK09558 | ushA | 2.17e-80 | 32 | 498 | 35 | 538 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| pfam02872 | 5_nucleotid_C | 9.29e-61 | 319 | 472 | 1 | 154 | 5'-nucleotidase, C-terminal domain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQY79959.1 | 6.71e-139 | 31 | 507 | 38 | 510 |
| QUH21387.1 | 2.73e-135 | 31 | 508 | 38 | 510 |
| ABW18467.1 | 8.29e-129 | 31 | 508 | 59 | 531 |
| QZY54554.1 | 9.74e-129 | 30 | 504 | 32 | 501 |
| ABR49732.1 | 6.37e-126 | 31 | 505 | 35 | 506 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3IVD_A | 5.91e-49 | 30 | 490 | 5 | 480 | Putative5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVD_B Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVE_A Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine [Escherichia coli O6] |
| 2Z1A_A | 9.11e-49 | 32 | 507 | 30 | 530 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 1USH_A | 6.34e-42 | 18 | 501 | 20 | 540 | 5'-NucleotidaseFrom E. Coli [Escherichia coli K-12],2USH_A 5'-Nucleotidase From E. Coli [Escherichia coli K-12],2USH_B 5'-Nucleotidase From E. Coli [Escherichia coli K-12] |
| 1HO5_A | 1.01e-40 | 24 | 501 | 1 | 515 | 5'-Nucleotidase(E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HO5_B 5'-Nucleotidase (E. Coli) In Complex With Adenosine And Phosphate [Escherichia coli],1HPU_A 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_B 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_C 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli],1HPU_D 5'-Nucleotidase (Closed Form), Complex With Ampcp [Escherichia coli] |
| 1HP1_A | 1.65e-40 | 24 | 501 | 1 | 506 | 5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A9BJC1 | 1.94e-60 | 32 | 491 | 24 | 481 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
| O34313 | 2.40e-59 | 31 | 505 | 668 | 1174 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| P29240 | 4.82e-51 | 31 | 505 | 31 | 546 | 5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1 |
| P22848 | 8.38e-45 | 18 | 500 | 24 | 542 | 5'-nucleotidase OS=Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) OX=223926 GN=nutA PE=3 SV=2 |
| Q61503 | 1.45e-44 | 31 | 505 | 30 | 548 | 5'-nucleotidase OS=Mus musculus OX=10090 GN=Nt5e PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.312731 | 0.677007 | 0.008306 | 0.000796 | 0.000439 | 0.000706 |
