Species | Leptotrichia wadei_A | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae; Leptotrichia; Leptotrichia wadei_A | |||||||||||
CAZyme ID | MGYG000002635_01180 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 453; End: 2042 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 266 | 384 | 1e-23 | 0.6941176470588235 |
GT2 | 15 | 118 | 1.3e-19 | 0.6647058823529411 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06420 | GT2_Chondriotin_Pol_N | 3.91e-84 | 267 | 487 | 1 | 182 | N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix. |
cd02511 | Beta4Glucosyltransferase | 6.92e-81 | 13 | 239 | 1 | 229 | UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core. |
pfam00535 | Glycos_transf_2 | 1.95e-22 | 266 | 374 | 1 | 106 | 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. |
COG0463 | WcaA | 3.41e-20 | 11 | 258 | 2 | 263 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd00761 | Glyco_tranf_GTA_type | 1.83e-19 | 268 | 373 | 2 | 104 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BBM55910.1 | 0.0 | 12 | 529 | 1 | 518 |
BBM41740.1 | 0.0 | 12 | 529 | 1 | 518 |
BBM43871.1 | 0.0 | 12 | 529 | 1 | 518 |
BBM48715.1 | 0.0 | 12 | 529 | 1 | 518 |
BBM50982.1 | 0.0 | 12 | 529 | 1 | 518 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7MSP_A | 6.53e-12 | 14 | 104 | 56 | 149 | ChainA, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168],7MSP_B Chain B, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168] |
7MSN_A | 1.05e-11 | 14 | 104 | 56 | 149 | ChainA, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168],7MSN_B Chain B, SPbeta prophage-derived glycosyltransferase SunS [Bacillus subtilis subsp. subtilis str. 168] |
5HEA_A | 1.26e-07 | 262 | 365 | 4 | 103 | 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] |
7MSK_A | 1.58e-07 | 14 | 108 | 68 | 167 | ChainA, Glyco_trans_2-like domain-containing protein [Bacillus thuringiensis serovar andalousiensis BGSC 4AW1],7MSK_B Chain B, Glyco_trans_2-like domain-containing protein [Bacillus thuringiensis serovar andalousiensis BGSC 4AW1] |
5TZE_C | 4.14e-07 | 266 | 366 | 4 | 103 | Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P44029 | 1.07e-37 | 14 | 255 | 4 | 248 | Uncharacterized glycosyltransferase HI_0653 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0653 PE=3 SV=1 |
Q1RJ60 | 3.95e-36 | 13 | 255 | 8 | 261 | Uncharacterized glycosyltransferase RBE_0523 OS=Rickettsia bellii (strain RML369-C) OX=336407 GN=RBE_0523 PE=3 SV=1 |
Q4UMM0 | 2.51e-32 | 13 | 255 | 3 | 256 | Uncharacterized glycosyltransferase RF_0337 OS=Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) OX=315456 GN=RF_0337 PE=3 SV=1 |
Q68XF1 | 8.05e-32 | 11 | 255 | 1 | 256 | Uncharacterized glycosyltransferase RT0209 OS=Rickettsia typhi (strain ATCC VR-144 / Wilmington) OX=257363 GN=RT0209 PE=3 SV=1 |
Q9XC90 | 1.31e-31 | 13 | 253 | 4 | 245 | Lipopolysaccharide core biosynthesis glycosyltransferase WaaE OS=Klebsiella pneumoniae OX=573 GN=waaE PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000038 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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