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CAZyme Information: MGYG000000170_00397
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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 | Alistipes_A sp900240235 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235 | |||||||||||
| CAZyme ID | MGYG000000170_00397 | |||||||||||
| CAZy Family | GT94 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 457488; End: 458666 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT94 | 117 | 315 | 1.3e-17 | 0.6431095406360424 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03822 | GT4_mannosyltransferase-like | 1.07e-28 | 9 | 379 | 4 | 370 | mannosyltransferases of glycosyltransferase family 4 and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides. |
| COG0438 | RfaB | 9.18e-27 | 4 | 384 | 1 | 380 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd03801 | GT4_PimA-like | 1.36e-23 | 5 | 379 | 1 | 366 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. |
| pfam00534 | Glycos_transf_1 | 9.27e-15 | 238 | 360 | 35 | 157 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
| cd03821 | GT4_Bme6-like | 5.85e-14 | 106 | 375 | 101 | 376 | Brucella melitensis Bme6 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QGA24742.1 | 2.03e-291 | 4 | 392 | 1 | 389 |
| BCG53842.1 | 4.58e-195 | 2 | 381 | 7 | 386 |
| CBK64994.1 | 1.61e-149 | 1 | 378 | 1 | 386 |
| AFL79017.1 | 2.77e-144 | 9 | 381 | 5 | 377 |
| BBL07853.1 | 7.90e-144 | 9 | 381 | 5 | 377 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3C4Q_A | 3.01e-09 | 89 | 384 | 97 | 408 | Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum] |
| 3L01_A | 3.02e-09 | 199 | 378 | 248 | 427 | ChainA, GlgA glycogen synthase [Pyrococcus abyssi],3L01_B Chain B, GlgA glycogen synthase [Pyrococcus abyssi] |
| 3C48_A | 3.09e-09 | 89 | 384 | 117 | 428 | Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum] |
| 3FRO_A | 3.09e-09 | 199 | 378 | 248 | 427 | Crystalstructure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_B Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_C Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi] |
| 2BIS_A | 3.10e-09 | 199 | 378 | 249 | 428 | Structureof glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi],2BIS_B Structure of glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi],2BIS_C Structure of glycogen synthase from Pyrococcus abyssi [Pyrococcus abyssi] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D4GU66 | 9.43e-14 | 204 | 381 | 194 | 371 | Low-salt glycan biosynthesis hexosyltransferase Agl5 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=agl5 PE=3 SV=1 |
| D1BD84 | 2.95e-11 | 122 | 378 | 166 | 414 | D-inositol 3-phosphate glycosyltransferase OS=Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74) OX=446469 GN=mshA PE=3 SV=1 |
| D5UJ42 | 1.31e-09 | 163 | 383 | 233 | 441 | D-inositol 3-phosphate glycosyltransferase OS=Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / NCIMB 8073 / NRS 134) OX=446466 GN=mshA PE=3 SV=1 |
| Q6NJL3 | 9.33e-09 | 87 | 378 | 100 | 405 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) OX=257309 GN=mshA PE=3 SV=1 |
| Q8NTA6 | 1.62e-08 | 89 | 384 | 97 | 408 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1 |
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 |
|---|---|---|---|---|---|
| 1.000067 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |