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CAZyme Information: MGYG000001510_02419

You are here: Home > Sequence: MGYG000001510_02419

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 Numidum massiliense
Lineage Bacteria; Firmicutes; Bacilli; Thermoactinomycetales; Novibacillaceae; Numidum; Numidum massiliense
CAZyme ID MGYG000001510_02419
CAZy Family CBM50
CAZyme Description Trifunctional nucleotide phosphoesterase protein YfkN
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
569 MGYG000001510_9|CGC18 62297.96 4.5056
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001510 3755739 Isolate not provided not provided
Gene Location Start: 2479023;  End: 2480732  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001510_02419.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09419 PRK09419 2.10e-154 59 568 655 1152
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737 UshA 1.80e-125 63 564 25 516
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558 ushA 6.77e-121 59 552 29 538
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07409 MPP_CD73_N 1.91e-103 65 325 1 277
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.
cd00845 MPP_UshA_N_like 4.14e-72 65 327 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
QLL63164.1 9.04e-114 62 569 25 541
QFI67637.1 8.67e-113 62 568 25 540
CCE97351.1 1.36e-112 62 569 25 541
AWM26442.1 1.36e-112 62 569 25 541
APG92489.1 1.77e-112 62 569 25 541

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z1A_A 1.22e-136 61 559 26 528
Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
5H7W_A 7.95e-91 61 560 1 523
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]
7D0V_A 4.48e-90 61 560 1 523
ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]
6VC9_A 5.21e-83 63 559 1 520
TB19complex [Homo sapiens],6VCA_A TB38 complex [Homo sapiens],6VCA_B TB38 complex [Homo sapiens],6VCA_C TB38 complex [Homo sapiens],6VCA_D TB38 complex [Homo sapiens]
4H1Y_P 5.74e-83 58 559 19 543
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O34313 7.20e-145 51 562 655 1177
Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
B6EWW8 9.66e-91 61 560 40 562
Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 SV=1
P29240 1.02e-90 63 562 30 549
5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1
F8S0Z7 1.36e-90 61 560 40 562
Snake venom 5'-nucleotidase OS=Crotalus adamanteus OX=8729 PE=1 SV=2
A0A2I4HXH5 4.36e-90 61 560 1 523
Snake venom 5'-nucleotidase (Fragment) OS=Naja atra OX=8656 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000054 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001510_02419.