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CAZyme Information: MGYG000000765_00088
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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 | Porphyromonas_A bennonis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A bennonis | |||||||||||
| CAZyme ID | MGYG000000765_00088 | |||||||||||
| CAZy Family | GH89 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 107255; End: 109495 Strand: + | |||||||||||
Full Sequence Download help
| MKQKITLVLI LLLLPLITAC GNGSEEADEA IAPLIGLCDR LFPEKSGAFQ FVLDRDTTSL | 60 |
| DSPSRYSVVA ERGKVTVRGS DPLALSVGLN RYLSEYCHTY VSPYAYDKVE LPGRLPDTKG | 120 |
| PLEGSAVVPE RFFLNYCTFG YSMPYWKWAD WERLIDWMAL QGVTMPLAIT GQEKVWLDVW | 180 |
| TELGLNPESV KSYFTGPAHL PWHRMNNIDR WEGPLPDSWL DEQVELQKKI LERERSFGMT | 240 |
| PVLPAFAGHV PQELAQHYPD AEVLRLGEWG GFEEKYGTYY LSPASPLFRK IQTLYLEKQT | 300 |
| ELFGTDHIYG IDAFNEVDSP DWSPEFLADV SRAIHTSLTD VDSEAKWLMM TWLFYYDKEH | 360 |
| WTPERIRAFL EAVPRGSIYL LDYYCDKAEV WRETEAFYGQ PYLWCYLGNF GGNSWLCGNM | 420 |
| RDVREKLSAA QATPSSAPMG IGCTLEGLDA NPIMYEYVLS QAWTSAPTAD DWIRIWADKR | 480 |
| GNSSANNYVY EAWKILESSV YRDFSRGGQA VLIHARPCLH GYQGWCTVPD YEYDNDDLLR | 540 |
| AWQLLLQGYT SAESHHRELT YDLVNVGRQL LGNRFMELRD VLTKAYEDKD LDQVSAVGQQ | 600 |
| MKELMDDYAS LLTYEPYFTL GKWLRDARDY GSHSEAEADY YERNARSILT VWGQPGRQLT | 660 |
| DYANRAYAGL VTDYYAPRWK RFIESVESSL REGIPLDEEQ FRTEMIAFED QWRHSTGEIA | 720 |
| EVRPSMPIDR YVSLLISKYF PSGDSR | 746 |
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH89 | 72 | 718 | 3e-231 | 0.9683257918552036 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam05089 | NAGLU | 0.0 | 131 | 465 | 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 | 4.24e-72 | 472 | 716 | 1 | 242 | 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 | 9.29e-17 | 32 | 116 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUT70725.1 | 4.24e-273 | 24 | 736 | 5 | 709 |
| BCA49739.1 | 7.63e-272 | 37 | 736 | 1 | 692 |
| BCA49750.1 | 1.17e-269 | 16 | 720 | 13 | 706 |
| QUT70734.1 | 1.17e-269 | 16 | 720 | 13 | 706 |
| QMW87500.1 | 3.68e-269 | 10 | 712 | 8 | 699 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4XWH_A | 2.77e-157 | 25 | 741 | 1 | 713 | Crystalstructure of the human N-acetyl-alpha-glucosaminidase [Homo sapiens] |
| 2VC9_A | 1.02e-94 | 73 | 693 | 212 | 831 | 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 | 1.18e-94 | 73 | 693 | 220 | 839 | 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 | 1.12e-93 | 73 | 693 | 235 | 854 | CpGH89(E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose [Clostridium perfringens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P54802 | 6.17e-159 | 19 | 741 | 18 | 736 | Alpha-N-acetylglucosaminidase OS=Homo sapiens OX=9606 GN=NAGLU PE=1 SV=2 |
| Q9FNA3 | 6.68e-129 | 24 | 741 | 41 | 806 | Alpha-N-acetylglucosaminidase OS=Arabidopsis thaliana OX=3702 GN=NAGLU PE=2 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 | 0.000001 | 1.000048 | 0.000000 | 0.000000 | 0.000000 |