Species | Blautia_A obeum_B | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A obeum_B | |||||||||||
CAZyme ID | MGYG000000252_00261 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 235950; End: 238040 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 5 | 131 | 2.4e-35 | 0.7529411764705882 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam02397 | Bac_transf | 7.99e-59 | 516 | 688 | 1 | 180 | Bacterial sugar transferase. This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways. |
TIGR03025 | EPS_sugtrans | 1.40e-54 | 276 | 688 | 4 | 439 | exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase. Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model. |
COG2148 | WcaJ | 1.87e-49 | 508 | 688 | 33 | 220 | Sugar transferase involved in LPS biosynthesis (colanic, teichoic acid) [Cell wall/membrane/envelope biogenesis]. |
cd00761 | Glyco_tranf_GTA_type | 2.24e-37 | 6 | 123 | 1 | 118 | 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. |
cd04196 | GT_2_like_d | 2.78e-37 | 5 | 203 | 1 | 204 | Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL24103.1 | 0.0 | 1 | 696 | 1 | 696 |
AUM96479.1 | 4.74e-75 | 2 | 248 | 9 | 253 |
AVQ53931.1 | 4.74e-75 | 2 | 248 | 9 | 253 |
QNO13385.1 | 4.83e-73 | 4 | 248 | 8 | 250 |
ATL91301.1 | 2.66e-71 | 4 | 248 | 8 | 250 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5W7L_A | 6.94e-20 | 516 | 694 | 11 | 192 | Structureof Campylobacter concisus PglC I57M/Q175M variant [Campylobacter concisus 13826],5W7L_B Structure of Campylobacter concisus PglC I57M/Q175M variant [Campylobacter concisus 13826] |
5HEA_A | 1.21e-16 | 4 | 93 | 7 | 95 | CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213] |
1H7L_A | 1.28e-15 | 2 | 120 | 1 | 126 | dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis] |
2Z87_A | 2.77e-15 | 1 | 145 | 373 | 515 | Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli],2Z87_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GalNAc and UDP [Escherichia coli] |
2Z86_A | 2.78e-15 | 1 | 145 | 374 | 516 | Crystalstructure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_B Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_C Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli],2Z86_D Crystal structure of chondroitin polymerase from Escherichia coli strain K4 (K4CP) complexed with UDP-GlcUA and UDP [Escherichia coli] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O32268 | 5.11e-48 | 2 | 223 | 6 | 225 | Putative teichuronic acid biosynthesis glycosyltransferase TuaG OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaG PE=2 SV=1 |
B5L3F2 | 4.42e-36 | 4 | 249 | 6 | 245 | UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfgD OS=Escherichia coli OX=562 GN=wfgD PE=1 SV=1 |
Q57022 | 4.35e-29 | 1 | 248 | 3 | 248 | Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 PE=3 SV=1 |
Q077R2 | 7.13e-28 | 1 | 248 | 1 | 241 | UDP-Glc:alpha-D-GlcNAc-diphosphoundecaprenol beta-1,3-glucosyltransferase WfaP OS=Escherichia coli OX=562 GN=wfaP PE=1 SV=1 |
Q0P9D0 | 1.80e-23 | 512 | 694 | 3 | 187 | Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglC PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000053 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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371 | 393 |
522 | 544 |
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