| Species | Anaerocolumna aminovalerica | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerocolumna; Anaerocolumna aminovalerica | |||||||||||
| CAZyme ID | MGYG000002836_01752 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | Mannosylglucosyl-3-phosphoglycerate phosphatase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 14273; End: 16126 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09419 | PRK09419 | 2.27e-111 | 25 | 515 | 650 | 1153 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| COG0737 | UshA | 5.15e-111 | 7 | 509 | 1 | 516 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09558 | ushA | 6.79e-110 | 1 | 519 | 2 | 551 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| cd07408 | MPP_SA0022_N | 3.09e-72 | 40 | 274 | 1 | 235 | 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. |
| cd00845 | MPP_UshA_N_like | 1.17e-67 | 42 | 279 | 3 | 237 | Escherichia coli UshA-like family, N-terminal metallophosphatase domain. This family includes the bacterial enzyme UshA, and related enzymes including SoxB, CpdB, YhcR, and CD73. All members have a similar domain architecture which includes an N-terminal metallophosphatase domain and a C-terminal nucleotidase 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCJ95849.1 | 8.32e-226 | 1 | 614 | 1 | 623 |
| QQY79959.1 | 2.16e-161 | 2 | 617 | 6 | 577 |
| QZY54554.1 | 7.68e-153 | 41 | 617 | 35 | 575 |
| ABW18467.1 | 1.09e-151 | 11 | 614 | 31 | 601 |
| AOT71215.1 | 8.68e-151 | 41 | 612 | 42 | 610 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2Z1A_A | 2.95e-64 | 38 | 516 | 27 | 539 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 1HP1_A | 3.53e-56 | 35 | 493 | 4 | 498 | 5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli] |
| 1USH_A | 1.32e-55 | 18 | 493 | 13 | 532 | 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 | 1.56e-55 | 35 | 493 | 4 | 507 | 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] |
| 1OID_A | 2.48e-55 | 35 | 493 | 4 | 507 | 5'-Nucleotidase(E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OID_B 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli],1OIE_A 5'-Nucleotidase (E. coli) with an Engineered Disulfide Bridge (S228C, P513C) [Escherichia coli] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A9BJC1 | 1.86e-67 | 39 | 501 | 23 | 491 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
| O34313 | 2.12e-67 | 42 | 506 | 671 | 1175 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| Q56878 | 5.39e-56 | 35 | 493 | 29 | 532 | Protein UshA OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=ushA PE=3 SV=3 |
| P07024 | 7.25e-55 | 18 | 493 | 13 | 532 | Protein UshA OS=Escherichia coli (strain K12) OX=83333 GN=ushA PE=1 SV=2 |
| B6EWW8 | 5.28e-54 | 42 | 505 | 46 | 561 | Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000297 | 0.999007 | 0.000187 | 0.000171 | 0.000161 | 0.000153 |
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