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CAZyme Information: MGYG000002953_01003

You are here: Home > Sequence: MGYG000002953_01003

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 UMGS1202 sp900549565
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UMGS1202; UMGS1202 sp900549565
CAZyme ID MGYG000002953_01003
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1070 112671.81 4.1463
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002953 3706118 MAG United States North America
Gene Location Start: 26137;  End: 29349  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002953_01003.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0737 UshA 5.72e-83 9 520 1 504
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09558 ushA 5.68e-67 6 532 3 548
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
PRK09419 PRK09419 7.26e-67 27 519 651 1135
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
cd07408 MPP_SA0022_N 2.42e-55 37 290 1 252
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 2.36e-51 37 280 1 239
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
ADK79942.1 3.20e-103 709 1064 26 379
BCJ95849.1 1.59e-98 1 512 1 492
AMJ40401.1 2.70e-86 211 534 1 328
ABW18467.1 8.76e-83 3 512 27 514
AZH28348.1 5.97e-82 37 538 49 525

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z1A_A 8.49e-38 36 512 29 514
Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
3IVD_A 3.39e-33 33 491 3 459
Putative5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVD_B Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVE_A Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine [Escherichia coli O6]
4H2I_A 1.46e-32 39 513 6 508
Humanecto-5'-nucleotidase (CD73): crystal form III (closed) in complex with AMPCP [Homo sapiens],6TVX_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12676 (an AOPCP derivative, compound 9 in paper) in the closed state [Homo sapiens],6TW0_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12690 (an AOPCP derivative, compound 10 in publication) in the closed state [Homo sapiens],6TWA_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12646 (an AOPCP derivative, compound 20 in publication) in the closed state [Homo sapiens],6TWF_A Human CD73 (ecto 5'-nucleotidase) in complex with PSB12604 (an AOPCP derivative, compound 21 in publication) in the closed state [Homo sapiens],6YE1_A Chain A, 5'-nucleotidase [Homo sapiens],6YE1_B Chain B, 5'-nucleotidase [Homo sapiens],6YE2_A Chain A, 5'-nucleotidase [Homo sapiens],6YE2_B Chain B, 5'-nucleotidase [Homo sapiens],6Z9B_A Human Ecto-5'-nucleotidase (CD73) in complex with AOPCP derivative A830 (compound 16 in publication) in the closed form (crystal form III) [Homo sapiens]
6S7F_A 2.61e-32 39 513 6 508
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]
6XUE_A 2.80e-32 39 513 5 507
HumanEcto-5'-nucleotidase (CD73) in complex with A2396 (compound 74 in publication) in the closed form in crystal form IV [Homo sapiens],6XUE_B Human Ecto-5'-nucleotidase (CD73) in complex with A2396 (compound 74 in publication) in the closed form in crystal form IV [Homo sapiens],6XUG_A Human Ecto-5'-nucleotidase (CD73) in complex with A2410 (compound 53 in publication) in the closed form in crystal form IV [Homo sapiens],6XUG_B Human Ecto-5'-nucleotidase (CD73) in complex with A2410 (compound 53 in publication) in the closed form in crystal form IV [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 2.36e-42 28 521 660 1167
Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
A9BJC1 5.98e-40 6 499 3 468
Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
Q9XZ43 1.55e-34 24 534 21 560
Protein 5NUC OS=Lutzomyia longipalpis OX=7200 GN=5NUC PE=1 SV=1
Q9KQ30 9.57e-34 24 532 25 550
5'-nucleotidase OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=nutA PE=3 SV=1
Q05927 2.96e-32 39 513 31 533
5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E 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
0.000291 0.998812 0.000354 0.000191 0.000179 0.000155

TMHMM  Annotations      download full data without filtering help

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