Species | Campylobacter hyointestinalis | |||||||||||
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Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter; Campylobacter hyointestinalis | |||||||||||
CAZyme ID | MGYG000002307_00026 | |||||||||||
CAZy Family | GT0 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 30106; End: 31680 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3980 | SpsG | 7.53e-27 | 202 | 457 | 2 | 258 | Spore coat polysaccharide biosynthesis protein SpsG, predicted glycosyltransferase [Cell wall/membrane/envelope biogenesis]. |
cd02513 | CMP-NeuAc_Synthase | 4.16e-07 | 5 | 198 | 3 | 223 | CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety. CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm. |
COG1083 | NeuA | 5.09e-07 | 5 | 202 | 5 | 226 | CMP-N-acetylneuraminic acid synthetase [Cell wall/membrane/envelope biogenesis]. |
cd03785 | GT28_MurG | 8.73e-06 | 215 | 519 | 10 | 350 | 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 |
---|---|---|---|---|---|
ANE31748.1 | 0.0 | 1 | 524 | 1 | 524 |
QKF54913.1 | 0.0 | 1 | 524 | 1 | 524 |
ALV23648.1 | 0.0 | 1 | 524 | 1 | 524 |
SNB47013.1 | 4.26e-155 | 1 | 524 | 1 | 537 |
ABM29645.1 | 3.45e-123 | 6 | 524 | 8 | 535 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q58462 | 1.15e-27 | 209 | 455 | 9 | 272 | Uncharacterized protein MJ1062 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1062 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000042 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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