logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001491_02346

You are here: Home > Sequence: MGYG000001491_02346

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 Rubeoparvulum massiliense
Lineage Bacteria; Firmicutes; Bacilli; Rubeoparvulales; Rubeoparvulaceae; Rubeoparvulum; Rubeoparvulum massiliense
CAZyme ID MGYG000001491_02346
CAZy Family CBM50
CAZyme Description Mannosylglucosyl-3-phosphoglycerate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
606 MGYG000001491_6|CGC3 65433.6 4.7152
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001491 2843796 Isolate not provided not provided
Gene Location Start: 768991;  End: 770811  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001491_02346.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 561 604 9.7e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0737 UshA 1.86e-125 22 495 5 496
2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419 PRK09419 3.80e-125 28 499 645 1133
multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09558 ushA 4.19e-112 22 504 14 541
bifunctional UDP-sugar hydrolase/5'-nucleotidase periplasmic precursor; Reviewed
cd07408 MPP_SA0022_N 7.11e-78 44 284 1 247
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 3.88e-75 44 286 1 247
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
QZY54554.1 1.73e-199 13 605 9 574
AOT71215.1 1.09e-197 10 606 10 615
QQY79959.1 4.88e-197 10 605 6 576
AGA59602.1 1.08e-191 21 604 15 601
AEI45885.1 3.37e-188 38 604 43 592

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z1A_A 9.37e-75 43 477 29 495
Crystalstructure of 5'-nucleotidase precursor from Thermus thermophilus HB8 [Thermus thermophilus HB8]
4H2I_A 2.97e-63 44 498 4 511
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 2.97e-63 44 498 4 511
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 3.38e-63 44 498 3 510
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]
7JV9_A 3.54e-63 44 498 5 512
HumanCD73 (ecto 5'-nucleotidase) in complex with compound 12 [Homo sapiens],7JV9_B Human CD73 (ecto 5'-nucleotidase) in complex with compound 12 [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 2.72e-76 44 478 24 465
Mannosylglucosyl-3-phosphoglycerate phosphatase OS=Petrotoga mobilis (strain DSM 10674 / SJ95) OX=403833 GN=mggB PE=1 SV=1
O34313 1.97e-73 44 477 669 1141
Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
Q05927 1.05e-64 44 500 29 538
5'-nucleotidase OS=Bos taurus OX=9913 GN=NT5E PE=1 SV=2
P29240 1.56e-63 44 497 32 534
5'-nucleotidase OS=Diplobatis ommata OX=1870830 PE=2 SV=1
B6EWW8 5.21e-62 44 477 44 530
Snake venom 5'-nucleotidase OS=Gloydius brevicaudus OX=259325 PE=2 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
0.000245 0.999028 0.000215 0.000178 0.000166 0.000141

TMHMM  Annotations      download full data without filtering help

start end
13 35