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CAZyme Information: MGYG000002421_01417
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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 | CABMKH01 sp902386935 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Tissierellales; Tissierellaceae; CABMKH01; CABMKH01 sp902386935 | |||||||||||
| CAZyme ID | MGYG000002421_01417 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | Mannosylglucosyl-3-phosphoglycerate phosphatase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 325061; End: 326905 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| PRK09419 | PRK09419 | 5.71e-125 | 19 | 521 | 640 | 1154 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| COG0737 | UshA | 1.10e-124 | 14 | 502 | 1 | 501 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09558 | ushA | 1.80e-121 | 5 | 505 | 1 | 540 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| cd00845 | MPP_UshA_N_like | 7.68e-71 | 40 | 294 | 1 | 255 | 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. |
| cd07408 | MPP_SA0022_N | 1.99e-61 | 41 | 284 | 2 | 246 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QQY79959.1 | 1.35e-216 | 1 | 614 | 1 | 575 |
| AOT71215.1 | 9.49e-172 | 29 | 614 | 28 | 613 |
| AGA59602.1 | 4.67e-163 | 7 | 614 | 9 | 601 |
| QUH21387.1 | 1.63e-160 | 3 | 614 | 5 | 587 |
| ABW18467.1 | 1.49e-159 | 4 | 614 | 27 | 602 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2Z1A_A | 1.09e-75 | 40 | 512 | 30 | 530 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 4H2F_A | 4.74e-62 | 33 | 511 | 19 | 544 | Humanecto-5'-nucleotidase (CD73): crystal form I (open) in complex with adenosine [Homo sapiens],4H2G_A Human ecto-5'-nucleotidase (CD73): crystal form II (open) in complex with adenosine [Homo sapiens] |
| 4H1Y_P | 6.59e-62 | 33 | 511 | 19 | 544 | Humanecto-5'-nucleotidase (CD73): crystal form II (open) in complex with PSB11552 [Homo sapiens],6TVE_P Unliganded human CD73 (5'-nucleotidase) in the open state [Homo sapiens],6TVG_A Human CD73 (ecto 5'-nucleotidase) in complex with AMPCP in the open state [Homo sapiens],7BBJ_A Chain A, 5'-nucleotidase [Homo sapiens],7BBJ_B Chain B, 5'-nucleotidase [Homo sapiens],7P9N_A Chain A, 5'-nucleotidase [Homo sapiens],7P9R_A Chain A, 5'-nucleotidase [Homo sapiens],7P9T_A Chain A, 5'-nucleotidase [Homo sapiens],7PA4_A Chain A, 5'-nucleotidase [Homo sapiens],7PB5_A Chain A, 5'-nucleotidase [Homo sapiens],7PBA_A Chain A, 5'-nucleotidase [Homo sapiens],7PBB_A Chain A, 5'-nucleotidase [Homo sapiens],7PBY_A Chain A, 5'-nucleotidase [Homo sapiens],7PCP_A Chain A, 5'-nucleotidase [Homo sapiens],7PD9_A Chain A, 5'-nucleotidase [Homo sapiens] |
| 1HP1_A | 9.27e-62 | 39 | 506 | 8 | 506 | 5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli] |
| 6S7F_A | 9.45e-62 | 39 | 511 | 3 | 522 | HumanCD73 (5'-nucleotidase) in complex with PSB12379 (an AOPCP derivative) in the closed state [Homo sapiens],6S7H_A Human CD73 (5'-nucleotidase) in complex with PSB12489 (an AOPCP derivative) in the closed state [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A9BJC1 | 3.02e-88 | 6 | 502 | 2 | 487 | Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1 |
| O34313 | 7.14e-69 | 40 | 511 | 669 | 1175 | Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1 |
| P29240 | 3.41e-68 | 39 | 519 | 31 | 555 | 5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1 |
| F8S0Z7 | 3.19e-62 | 39 | 510 | 43 | 561 | Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2 |
| P07024 | 1.05e-60 | 14 | 506 | 9 | 540 | Protein UshA OS=Escherichia coli (strain K12) OX=83333 GN=ushA 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 |
|---|---|---|---|---|---|
| 0.000447 | 0.998729 | 0.000206 | 0.000252 | 0.000180 | 0.000149 |
