Species | Cetobacterium_A sp900766645 | |||||||||||
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Lineage | Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Cetobacterium_A; Cetobacterium_A sp900766645 | |||||||||||
CAZyme ID | MGYG000000536_00732 | |||||||||||
CAZy Family | CBM50 | |||||||||||
CAZyme Description | Mannosylglucosyl-3-phosphoglycerate phosphatase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 12781; End: 14334 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0737 | UshA | 1.35e-115 | 6 | 502 | 1 | 499 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
PRK09419 | PRK09419 | 1.51e-112 | 21 | 517 | 650 | 1151 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
PRK09558 | ushA | 7.71e-109 | 1 | 502 | 1 | 535 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
cd07408 | MPP_SA0022_N | 2.98e-66 | 33 | 286 | 2 | 252 | 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 | 4.40e-63 | 32 | 277 | 1 | 240 | 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 |
---|---|---|---|---|---|
QQY79959.1 | 3.03e-145 | 31 | 509 | 38 | 510 |
AGF93428.1 | 3.98e-139 | 29 | 512 | 28 | 489 |
QZY54554.1 | 2.69e-137 | 29 | 502 | 31 | 492 |
AGA59602.1 | 3.81e-132 | 7 | 515 | 16 | 510 |
AEI45885.1 | 2.32e-128 | 18 | 502 | 39 | 508 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z1A_A | 5.59e-67 | 28 | 509 | 26 | 530 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
1HP1_A | 2.28e-60 | 26 | 500 | 3 | 498 | 5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli] |
1HO5_A | 1.06e-58 | 26 | 500 | 3 | 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 | 1.71e-58 | 26 | 500 | 3 | 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] |
1USH_A | 1.76e-58 | 26 | 500 | 28 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A9BJC1 | 2.29e-75 | 28 | 514 | 20 | 497 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
O34313 | 1.18e-71 | 25 | 517 | 662 | 1182 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
Q56878 | 4.74e-61 | 26 | 500 | 28 | 532 | Protein UshA OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) OX=393305 GN=ushA PE=3 SV=3 |
Q9RN37 | 1.31e-59 | 12 | 500 | 7 | 532 | Protein UshA OS=Salmonella pullorum OX=605 GN=ushA PE=3 SV=1 |
P06196 | 3.53e-59 | 12 | 500 | 7 | 532 | Silent protein UshA(0) OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=ushA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000000 | 1.000046 | 0.000000 | 0.000000 | 0.000000 |
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