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CAZyme Information: MGYG000002827_04066
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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 | Phyllobacterium sp900539805 | |||||||||||
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| Lineage | Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales_A; Rhizobiaceae_A; Phyllobacterium; Phyllobacterium sp900539805 | |||||||||||
| CAZyme ID | MGYG000002827_04066 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | Trifunctional nucleotide phosphoesterase protein YfkN | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 10261; End: 12120 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd07409 | MPP_CD73_N | 6.83e-131 | 28 | 310 | 1 | 279 | CD73 ecto-5'-nucleotidase and related proteins, N-terminal metallophosphatase domain. CD73 is a mammalian ecto-5'-nucleotidase expressed in endothelial cells and lymphocytes that catalyzes the conversion of 5'-AMP to adenosine in the final step of a pathway that generates adenosine from ATP. This pathway also includes a CD39 nucleoside triphosphate dephosphorylase that mediates the dephosphorylation of ATP to ADP and then to 5'-AMP. These enzymes all have an N-terminal metallophosphatase domain and a C-terminal 5'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. |
| COG0737 | UshA | 2.86e-118 | 1 | 535 | 1 | 514 | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms]. |
| PRK09419 | PRK09419 | 2.39e-108 | 27 | 534 | 660 | 1144 | multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase. |
| PRK09558 | ushA | 1.64e-86 | 7 | 524 | 3 | 536 | bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed |
| cd00845 | MPP_UshA_N_like | 5.19e-67 | 28 | 311 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ATU90724.1 | 0.0 | 1 | 617 | 1 | 628 |
| ASY64256.1 | 9.35e-265 | 9 | 619 | 39 | 655 |
| CAD6408460.1 | 1.76e-262 | 1 | 617 | 1 | 643 |
| CAD6616220.1 | 1.98e-260 | 1 | 619 | 1 | 660 |
| CCF20451.1 | 1.98e-260 | 1 | 619 | 1 | 660 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2Z1A_A | 8.30e-127 | 22 | 536 | 24 | 531 | Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
| 5H7W_A | 2.61e-115 | 25 | 533 | 2 | 522 | Crystalstructure of 5'-nucleotidase from venom of Naja atra [Naja atra],5H7W_B Crystal structure of 5'-nucleotidase from venom of Naja atra [Naja atra] |
| 4H1Y_P | 1.21e-114 | 26 | 533 | 24 | 543 | 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] |
| 4H2B_A | 1.25e-114 | 26 | 533 | 25 | 544 | Humanecto-5'-nucleotidase (CD73): crystal form II (open) in complex with Baicalin [Homo sapiens] |
| 7QGA_A | 3.50e-114 | 26 | 533 | 1 | 520 | ChainA, 5'-nucleotidase [Homo sapiens],7QGL_A Chain A, 5'-nucleotidase [Homo sapiens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A0A2I4HXH5 | 1.43e-114 | 25 | 533 | 2 | 522 | Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1 |
| Q05927 | 1.07e-113 | 22 | 533 | 23 | 546 | 5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E PE=1 SV=2 |
| B6EWW8 | 2.25e-113 | 22 | 533 | 38 | 561 | Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1 |
| P29240 | 2.54e-112 | 24 | 541 | 28 | 554 | 5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1 |
| P21589 | 3.29e-112 | 22 | 533 | 23 | 546 | 5'-nucleotidase OS=Homo sapiens OX=9606 GN=NT5E PE=1 SV=1 |
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 |
|---|---|---|---|---|---|
| 0.001132 | 0.997927 | 0.000272 | 0.000224 | 0.000204 | 0.000203 |
