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CAZyme Information: MGYG000004151_04903
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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 | Pseudomonas citronellolis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas; Pseudomonas citronellolis | |||||||||||
| CAZyme ID | MGYG000004151_04903 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | Alginate biosynthesis protein AlgA | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2807; End: 4252 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG0836 | CpsB | 0.0 | 1 | 332 | 2 | 333 | Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]. |
| PRK15460 | cpsB | 0.0 | 1 | 468 | 6 | 477 | mannose-1-phosphate guanyltransferase; Provisional |
| TIGR01479 | GMP_PMI | 0.0 | 1 | 468 | 1 | 468 | mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides] |
| cd02509 | GDP-M1P_Guanylyltransferase | 1.54e-139 | 1 | 277 | 1 | 274 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose. GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes. |
| pfam01050 | MannoseP_isomer | 4.02e-99 | 314 | 464 | 1 | 151 | Mannose-6-phosphate isomerase. All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGN91810.2 | 5.76e-168 | 1 | 467 | 2 | 472 |
| ACC75758.1 | 2.65e-53 | 1 | 273 | 32 | 312 |
| BCF92878.1 | 6.20e-53 | 1 | 291 | 29 | 327 |
| ABK18998.1 | 5.82e-23 | 345 | 468 | 319 | 443 |
| AKB32685.1 | 6.44e-23 | 362 | 469 | 320 | 427 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2QH5_A | 4.38e-60 | 4 | 290 | 8 | 288 | Crystalstructure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695],2QH5_B Crystal structure of mannose-6-phosphate isomerase from Helicobacter pylori [Helicobacter pylori 26695] |
| 2X5S_A | 1.90e-59 | 1 | 346 | 2 | 332 | Crystalstructure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5S_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in apo state. [Thermotoga maritima MSB8],2X5Z_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X5Z_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GDP-mannose. [Thermotoga maritima MSB8],2X60_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X60_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with GTP. [Thermotoga maritima MSB8],2X65_A Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8],2X65_B Crystal structure of T. maritima GDP-mannose pyrophosphorylase in complex with mannose-1-phosphate. [Thermotoga maritima MSB8] |
| 2CU2_A | 4.36e-57 | 4 | 348 | 6 | 335 | Crystalstructure of mannose-1-phosphate geranyltransferase from Thermus thermophilus HB8 [Thermus thermophilus HB8] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P07874 | 1.87e-311 | 1 | 481 | 1 | 481 | Alginate biosynthesis protein AlgA OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=algA PE=1 SV=3 |
| Q88ND5 | 5.83e-293 | 1 | 469 | 2 | 470 | Alginate biosynthesis protein AlgA OS=Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) OX=160488 GN=algA PE=3 SV=1 |
| Q887Q9 | 6.36e-285 | 1 | 481 | 1 | 483 | Alginate biosynthesis protein AlgA OS=Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000) OX=223283 GN=algA PE=3 SV=1 |
| P59785 | 2.46e-282 | 1 | 469 | 1 | 469 | Alginate biosynthesis protein AlgA OS=Pseudomonas fluorescens OX=294 GN=algA PE=3 SV=1 |
| B0RVK6 | 6.32e-201 | 1 | 469 | 4 | 467 | Xanthan biosynthesis protein XanB OS=Xanthomonas campestris pv. campestris (strain B100) OX=509169 GN=xanB 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 |
|---|---|---|---|---|---|
| 1.000079 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |