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CAZyme Information: MGYG000003002_00766
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Streptococcus sanguinis_H | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus sanguinis_H | |||||||||||
| CAZyme ID | MGYG000003002_00766 | |||||||||||
| CAZy Family | GT8 | |||||||||||
| CAZyme Description | Glycosyltransferase stabilizing protein Gtf2 | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 16468; End: 17334 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd04647 | LbH_MAT_like | 5.20e-38 | 43 | 141 | 2 | 101 | 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. |
| cd03357 | LbH_MAT_GAT | 6.10e-26 | 40 | 142 | 60 | 162 | Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). |
| COG0110 | WbbJ | 4.60e-24 | 4 | 152 | 23 | 178 | Acetyltransferase (isoleucine patch superfamily) [General function prediction only]. |
| PRK09677 | PRK09677 | 5.28e-23 | 32 | 152 | 50 | 184 | putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional |
| cd03354 | LbH_SAT | 6.50e-16 | 44 | 141 | 10 | 97 | Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SQG29868.1 | 3.54e-197 | 1 | 288 | 1 | 288 |
| QKQ44256.1 | 1.44e-196 | 1 | 288 | 1 | 288 |
| SQF34213.1 | 9.73e-195 | 1 | 288 | 1 | 288 |
| SQF71729.1 | 2.19e-191 | 1 | 288 | 1 | 288 |
| VDY72311.1 | 5.16e-190 | 1 | 288 | 1 | 288 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5E9U_B | 2.66e-16 | 159 | 275 | 288 | 405 | Crystalstructure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_D Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_F Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_H Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii] |
| 5E9T_B | 2.67e-16 | 159 | 275 | 288 | 405 | Crystalstructure of GtfA/B complex [Streptococcus gordonii],5E9T_D Crystal structure of GtfA/B complex [Streptococcus gordonii] |
| 5GVW_A | 3.44e-12 | 162 | 283 | 283 | 406 | Crystalstructure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_B Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_C Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVW_D Crystal structure of the apo-form glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae] |
| 5GVV_A | 1.13e-11 | 162 | 255 | 283 | 375 | Crystalstructure of the glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae],5GVV_F Crystal structure of the glycosyltransferase GlyE in Streptococcus pneumoniae TIGR4 [Streptococcus pneumoniae] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A0A0H2URA3 | 3.17e-17 | 140 | 284 | 265 | 404 | Glycosyltransferase GlyB OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyB PE=3 SV=1 |
| Q3S2Y1 | 2.34e-16 | 150 | 260 | 277 | 386 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB OS=Streptococcus agalactiae OX=1311 GN=gtfB PE=1 SV=1 |
| Q79T00 | 5.95e-16 | 159 | 275 | 288 | 405 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB OS=Streptococcus gordonii OX=1302 GN=gtfB PE=1 SV=1 |
| A0A0H2URH2 | 1.21e-15 | 131 | 281 | 243 | 395 | Glycosyltransferase GlyF OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyF PE=3 SV=1 |
| A0A0H2URH7 | 8.73e-15 | 157 | 283 | 570 | 696 | Glycosyltransferase GlyA OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |