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CAZyme Information: MGYG000004151_04903

You are here: Home > Sequence: MGYG000004151_04903

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
Protein Length CGC Molecular Weight Isoelectric Point
481 MGYG000004151_80|CGC1 53457.76 5.5836
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004151 7110046 MAG United Kingdom Europe
Gene Location Start: 2807;  End: 4252  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004151_04903.

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004151_04903.