Species | Vibrio cholerae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Vibrionaceae; Vibrio; Vibrio cholerae | |||||||||||
CAZyme ID | MGYG000002311_02087 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2346759; End: 2347847 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR00661 | MJ1255 | 0.0 | 2 | 311 | 1 | 321 | conserved hypothetical protein. This model represents nearly the full length of MJ1255 from Methanococcus jannaschii and of an unpublished protein from Vibrio cholerae, as well as the C-terminal half of a protein from Methanobacterium thermoautotrophicum. A small region (~50 amino acids) within the domain appears related to a family of sugar transferases. [Hypothetical proteins, Conserved] |
COG1819 | YjiC | 3.79e-73 | 1 | 362 | 2 | 398 | UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]. |
pfam13528 | Glyco_trans_1_3 | 5.32e-32 | 1 | 282 | 1 | 298 | Glycosyl transferase family 1. |
cd03785 | GT28_MurG | 2.92e-04 | 2 | 152 | 1 | 149 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AAF95629.1 | 3.25e-278 | 1 | 362 | 1 | 362 |
BBE11592.1 | 3.25e-278 | 1 | 362 | 1 | 362 |
SPM15092.1 | 3.25e-278 | 1 | 362 | 1 | 362 |
SPM20365.1 | 3.25e-278 | 1 | 362 | 1 | 362 |
ARB82492.1 | 3.25e-278 | 1 | 362 | 1 | 362 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000053 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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