Species | Prevotella sp900548535 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548535 | |||||||||||
CAZyme ID | MGYG000000553_01289 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 70353; End: 71555 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 2 | 113 | 6.1e-17 | 0.6705882352941176 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06433 | GT_2_WfgS_like | 2.07e-53 | 1 | 183 | 17 | 199 | WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. |
cd04647 | LbH_MAT_like | 4.65e-27 | 279 | 382 | 2 | 109 | Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form. |
PRK10502 | PRK10502 | 1.63e-24 | 235 | 387 | 25 | 180 | putative acyl transferase; Provisional |
cd05825 | LbH_wcaF_like | 9.93e-23 | 276 | 382 | 1 | 107 | wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms. |
COG0110 | WbbJ | 5.96e-22 | 224 | 388 | 12 | 181 | Acetyltransferase (isoleucine patch superfamily) [General function prediction only]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AXV50072.1 | 4.22e-156 | 1 | 400 | 22 | 421 |
QUB91771.1 | 8.48e-156 | 1 | 400 | 22 | 421 |
QUI93290.1 | 1.70e-155 | 1 | 400 | 22 | 421 |
QJR60740.1 | 5.02e-56 | 1 | 204 | 22 | 225 |
QJR54460.1 | 5.02e-56 | 1 | 204 | 22 | 225 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ECT_A | 5.26e-13 | 250 | 387 | 48 | 188 | CrystalStructure of the Hexapeptide-Repeat Containing-Acetyltransferase VCA0836 from Vibrio cholerae [Vibrio cholerae],3NZ2_A Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_B Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_C Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_D Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_E Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_F Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_G Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_H Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_I Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_J Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_K Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_L Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961] |
4MZU_A | 4.32e-12 | 287 | 383 | 31 | 148 | Crystalstructure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_B Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_C Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_D Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_E Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_F Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_G Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_H Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_I Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_J Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_K Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217],4MZU_L Crystal structure of FdtD, a bifunctional ketoisomerase/N-acetyltransferase from Shewanella denitrificans [Shewanella denitrificans OS217] |
1KQA_A | 7.02e-12 | 250 | 382 | 47 | 182 | GalactosideAcetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_B Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_C Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KRR_A Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_B Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_C Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRU_A Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_B Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_C Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRV_A Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_B Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_C Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli] |
3FTT_A | 1.64e-11 | 277 | 389 | 73 | 188 | ChainA, Putative acetyltransferase SACOL2570 [Staphylococcus aureus subsp. aureus COL] |
5U2K_A | 3.02e-11 | 277 | 389 | 73 | 188 | ChainA, Galactoside O-acetyltransferase [Staphylococcus aureus subsp. aureus COL] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P71239 | 4.82e-18 | 13 | 184 | 35 | 202 | Putative colanic acid biosynthesis glycosyl transferase WcaE OS=Escherichia coli (strain K12) OX=83333 GN=wcaE PE=4 SV=2 |
Q09707 | 1.05e-17 | 279 | 384 | 95 | 203 | Putative acetyltransferase C18B11.09c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC18B11.09c PE=3 SV=2 |
Q86A05 | 7.23e-14 | 279 | 382 | 81 | 189 | Putative acetyltransferase DDB_G0275507 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0275507 PE=3 SV=1 |
P37515 | 2.34e-12 | 279 | 380 | 75 | 179 | Probable maltose O-acetyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=maa PE=3 SV=1 |
P9WMX8 | 1.07e-11 | 13 | 159 | 37 | 183 | Uncharacterized glycosyltransferase MT1564 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1564 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000037 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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