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CAZyme Information: MGYG000004430_01631

You are here: Home > Sequence: MGYG000004430_01631

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485;
CAZyme ID MGYG000004430_01631
CAZy Family GH89
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1120 MGYG000004430_14|CGC2 127063.25 6.9703
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004430 3945500 MAG Israel Asia
Gene Location Start: 26595;  End: 29957  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004430_01631.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH89 463 1107 2.6e-236 0.9773755656108597

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05089 NAGLU 5.44e-179 521 850 1 333
Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This central domain has a tim barrel fold.
pfam12972 NAGLU_C 1.64e-84 858 1113 1 257
Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This C-terminal domain has an all alpha helical fold.
pfam12971 NAGLU_N 9.21e-28 428 506 1 81
Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain. Alpha-N-acetylglucosaminidase, a lysosomal enzyme required for the stepwise degradation of heparan sulfate. Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterized by neurological dysfunction but relatively mild somatic manifestations. The structure shows that the enzyme is composed of three domains. This N-terminal domain has an alpha-beta fold.
pfam00328 His_Phos_2 1.28e-11 73 396 10 353
Histidine phosphatase superfamily (branch 2). The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches.The smaller branch 2 contains predominantly eukaryotic proteins. The catalytic functions in members include phytase, glucose-1-phosphatase and multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in branch 2 are not fully understood, although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated.
cd07061 HP_HAP_like 1.16e-08 124 378 17 222
Histidine phosphatase domain found in histidine acid phosphatases and phytases; contains a His residue which is phosphorylated during the reaction. Catalytic domain of HAP (histidine acid phosphatases) and phytases (myo-inositol hexakisphosphate phosphohydrolases). The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. Functions in this subgroup include roles in metabolism, signaling, or regulation, for example Escherichia coli glucose-1-phosphatase functions to scavenge glucose from glucose-1-phosphate and the signaling molecules inositol 1,3,4,5,6-pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) are in vivo substrates for eukaryotic multiple inositol polyphosphate phosphatase 1 (Minpp1). Phytases scavenge phosphate from extracellular sources and are added to animal feed while prostatic acid phosphatase (PAP) has been used for many years as a serum marker for prostate cancer. Recently PAP has been shown in mouse models to suppress pain by functioning as an ecto-5prime-nucleotidase. In vivo it dephosphorylates extracellular adenosine monophosphate (AMP) generating adenosine,and leading to the activation of A1-adenosine receptors in dorsal spinal cord.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT50280.1 1.07e-301 426 1102 18 696
QRO24616.1 4.29e-301 428 1120 20 715
QTO27209.1 8.30e-288 428 1102 21 698
QCQ31494.1 1.66e-287 428 1102 21 698
QCQ35767.1 1.66e-287 428 1102 21 698

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VC9_A 1.74e-152 428 1099 172 850
Family89 Glycoside Hydrolase from Clostridium perfringens in complex with 2-acetamido-1,2-dideoxynojirmycin [Clostridium perfringens],2VCA_A Family 89 glycoside hydrolase from Clostridium perfringens in complex with beta-N-acetyl-D-glucosamine [Clostridium perfringens],2VCB_A Family 89 Glycoside Hydrolase from Clostridium perfringens in complex with PUGNAc [Clostridium perfringens],2VCC_A Family 89 Glycoside Hydrolase from Clostridium perfringens [Clostridium perfringens]
7MFK_A 2.16e-152 428 1099 180 858
ChainA, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124],7MFL_A Chain A, Alpha-N-acetylglucosaminidase family protein [Clostridium perfringens ATCC 13124]
4A4A_A 2.44e-151 428 1099 195 873
CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens]
4XWH_A 2.89e-114 468 1115 54 706
Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens]
7R5Y_A 1.16e-49 32 430 7 406
ChainA, Histidine acid phosphatase [Prevotella sp. CAG:617],7R5Y_B Chain B, Histidine acid phosphatase [Prevotella sp. CAG:617],7R5Y_C Chain C, Histidine acid phosphatase [Prevotella sp. CAG:617],7R5Y_D Chain D, Histidine acid phosphatase [Prevotella sp. CAG:617],7R5Y_E Chain E, Histidine acid phosphatase [Prevotella sp. CAG:617],7R5Y_F Chain F, Histidine acid phosphatase [Prevotella sp. CAG:617]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9FNA3 8.73e-124 433 1113 69 797
Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 SV=1
P54802 2.89e-113 468 1115 77 729
Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.608274 0.389194 0.001086 0.000814 0.000343 0.000294

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004430_01631.