Species | Haemophilus_A parahaemolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_A; Haemophilus_A parahaemolyticus | |||||||||||
CAZyme ID | MGYG000004687_01205 | |||||||||||
CAZy Family | GT80 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4006; End: 5226 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT80 | 8 | 392 | 5.1e-72 | 0.9947229551451188 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam11477 | PM0188 | 2.74e-89 | 9 | 390 | 1 | 384 | Sialyltransferase PMO188. PMO188 is a sialyltransferase from P.multocida. It transfers sialic acid from cytidine 5'-monophosphonuraminic acid to an acceptor sugar. It has important catalytic residues such as Asp141, His311, Glu338, Ser355 and Ser356. |
pfam07388 | A-2_8-polyST | 0.002 | 171 | 347 | 132 | 307 | Alpha-2,8-polysialyltransferase (POLYST). This family contains the bacterial enzyme alpha-2,8-polysialyltransferase (EC:2.4.99.-) (approximately 500 residues long). This catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEN11339.1 | 4.91e-284 | 1 | 406 | 1 | 406 |
QRP12533.1 | 4.91e-284 | 1 | 406 | 1 | 406 |
QLB20464.1 | 9.62e-103 | 7 | 401 | 7 | 402 |
AUI65092.1 | 2.52e-89 | 1 | 396 | 1 | 398 |
AKO30250.1 | 1.03e-80 | 7 | 380 | 5 | 381 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4V39_A | 6.77e-52 | 7 | 401 | 2 | 385 | Apo-structureof alpha2,3-sialyltransferase variant 2 from Pasteurella dagmatis [Pasteurella dagmatis],4V3C_A The structure of alpha2,3-sialyltransferase variant 2 from Pasteurella dagmatis in complex with the donor product CMP [Pasteurella dagmatis] |
4V38_A | 9.48e-52 | 7 | 401 | 2 | 385 | Apo-structureof alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis [Pasteurella dagmatis],4V3B_A The structure of alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis in complex with the donor product CMP [Pasteurella dagmatis] |
4V2U_A | 5.10e-51 | 7 | 401 | 2 | 385 | Apo-structureof alpha2,3-sialyltransferase from Pasteurella dagmatis [Pasteurella dagmatis] |
3S44_A | 1.81e-50 | 6 | 401 | 1 | 385 | CrystalStructure of Pasteurella multocida sialyltransferase M144D mutant with CMP bound [Pasteurella multocida] |
2EX0_A | 6.91e-50 | 6 | 401 | 1 | 385 | Crystalstructure of multifunctional sialyltransferase from Pasteurella Multocida [Pasteurella multocida],2EX0_B Crystal structure of multifunctional sialyltransferase from Pasteurella Multocida [Pasteurella multocida],2IHJ_A crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac bound [Pasteurella multocida],2IHK_A crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F(equatorial)-Neu5Ac bound [Pasteurella multocida],2IHZ_A Crystal structure of multifunctional sialyltransferase from pasteurella multocida with CMP-3F-Neu5Ac and alpha-lactose bound [Pasteurella multocida],2IIQ_A Crystal structure of Pasteurella multocida sialyltransferase in an open conformation with CMP bound [Pasteurella multocida],2IIQ_B Crystal structure of Pasteurella multocida sialyltransferase in an open conformation with CMP bound [Pasteurella multocida] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000067 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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