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CAZyme Information: MGYG000002326_03186
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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 | Alkalihalobacillus alcalophilus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_H; Bacillaceae_D; Alkalihalobacillus; Alkalihalobacillus alcalophilus | |||||||||||
| CAZyme ID | MGYG000002326_03186 | |||||||||||
| CAZy Family | GH57 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 3488; End: 6268 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH57 | 8 | 425 | 3.1e-74 | 0.8224543080939948 |
| GT4 | 739 | 890 | 4.6e-40 | 0.94375 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG1543 | COG1543 | 0.0 | 2 | 518 | 1 | 503 | Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism]. |
| cd10792 | GH57N_AmyC_like | 0.0 | 4 | 407 | 1 | 412 | N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily. |
| cd03801 | GT4_PimA-like | 1.66e-92 | 539 | 913 | 1 | 362 | 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. |
| cd10816 | GH57N_BE_TK1436_like | 1.45e-91 | 4 | 407 | 1 | 423 | N-terminal catalytic domain of Gh57 branching enzyme TK 1436 and similar proteins. The subfamily is represented by a novel branching-enzyme TK1436 of hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Branching enzymes (BEs, EC 2.4.1.18) play a key role in synthesis of alpha-glucans and they generally are classified into glycoside hydrolase family 13 (GH13). However, TK1436 belongs to the GH57 family. It functions as a monomer and possesses BE activity. TK1436 is composed of a distorted N-terminal (beta/alpha)7-barrel domain and a C-terminal five alpha-helical domain, both of which participate in the formation of the active-site cleft. |
| COG0438 | RfaB | 3.22e-63 | 539 | 913 | 1 | 371 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ARK29379.1 | 0.0 | 1 | 920 | 2 | 922 |
| ADC50836.1 | 0.0 | 1 | 920 | 1 | 928 |
| BAB05134.1 | 0.0 | 1 | 912 | 1 | 909 |
| QOY36139.1 | 0.0 | 1 | 920 | 1 | 923 |
| ANX12902.1 | 0.0 | 1 | 926 | 1 | 928 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2B5D_X | 1.08e-114 | 4 | 502 | 3 | 509 | Crystalstructure of the novel alpha-amylase AmyC from Thermotoga maritima [Thermotoga maritima MSB8] |
| 3N8T_A | 4.98e-71 | 3 | 514 | 2 | 519 | ChainA, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N92_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N98_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis] |
| 5WU7_A | 1.41e-69 | 3 | 527 | 2 | 528 | Crystalstructure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],5WU7_B Crystal structure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3] |
| 3P0B_A | 2.13e-56 | 6 | 517 | 24 | 536 | Thermusthermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed [Thermus thermophilus] |
| 1UFA_A | 2.78e-54 | 6 | 517 | 4 | 516 | Crystalstructure of TT1467 from Thermus thermophilus HB8 [Thermus thermophilus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q59002 | 2.05e-69 | 539 | 913 | 2 | 378 | Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1 |
| Q5JDJ7 | 3.05e-69 | 3 | 514 | 2 | 519 | 1,4-alpha-glucan branching enzyme TK1436 OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1436 PE=1 SV=1 |
| Q5SH28 | 7.73e-56 | 6 | 517 | 4 | 516 | 1,4-alpha-glucan branching enzyme TTHA1902 OS=Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) OX=300852 GN=TTHA1902 PE=1 SV=1 |
| P9WMY9 | 1.62e-50 | 539 | 912 | 2 | 386 | Glycogen synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3032 PE=1 SV=1 |
| P9WMY8 | 1.62e-50 | 539 | 912 | 2 | 386 | Glycogen synthase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3116 PE=3 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 |
|---|---|---|---|---|---|
| 1.000090 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |