Species | Paenibacillus_B thiaminolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus | |||||||||||
CAZyme ID | MGYG000002490_03757 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 84424; End: 85908 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 205 | 332 | 7e-24 | 0.7470588235294118 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04647 | LbH_MAT_like | 2.72e-29 | 60 | 171 | 2 | 108 | 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. |
pfam00535 | Glycos_transf_2 | 6.85e-21 | 205 | 331 | 1 | 126 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
cd00761 | Glyco_tranf_GTA_type | 4.95e-20 | 206 | 318 | 1 | 111 | Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities. |
cd03349 | LbH_XAT | 6.68e-19 | 74 | 169 | 10 | 121 | Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. |
COG0110 | WbbJ | 7.25e-19 | 62 | 171 | 70 | 174 | Acetyltransferase (isoleucine patch superfamily) [General function prediction only]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDM42457.1 | 0.0 | 1 | 494 | 8 | 501 |
BBI32702.1 | 1.64e-264 | 1 | 493 | 1 | 473 |
QJD82898.1 | 1.13e-239 | 30 | 491 | 4 | 465 |
AJS57572.1 | 6.10e-163 | 3 | 489 | 2 | 489 |
BBI33988.1 | 2.25e-158 | 1 | 489 | 1 | 489 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4MZU_A | 2.96e-07 | 61 | 189 | 30 | 164 | 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] |
6YV7_B | 1.11e-06 | 200 | 263 | 40 | 103 | MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548] |
6YV7_A | 1.11e-06 | 200 | 263 | 41 | 104 | MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548] |
3EEV_A | 1.38e-06 | 113 | 169 | 103 | 159 | CrystalStructure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_B Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_C Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_A The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_B The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_C The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUB_A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the Complex with Crystal Violet [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_A The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_B The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_C The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961] |
6MFK_A | 1.95e-06 | 114 | 169 | 111 | 166 | ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P26401 | 3.53e-15 | 203 | 382 | 2 | 203 | Abequosyltransferase RfbV OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=rfbV PE=1 SV=2 |
P37750 | 2.89e-10 | 60 | 182 | 68 | 193 | Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ OS=Escherichia coli (strain K12) OX=83333 GN=wbbJ PE=3 SV=2 |
P9WMX7 | 4.36e-08 | 202 | 328 | 4 | 131 | PGL/p-HBAD biosynthesis glycosyltransferase Rv2957 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2957 PE=1 SV=1 |
P0A5A0 | 4.36e-08 | 202 | 328 | 4 | 131 | PGL/p-HBAD biosynthesis glycosyltransferase Mb2981 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB2981 PE=3 SV=1 |
P9WMX6 | 4.36e-08 | 202 | 328 | 4 | 131 | PGL/p-HBAD biosynthesis glycosyltransferase MT3031 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3031 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000046 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.