Species | Paenibacillus_F sp000411255 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_F; Paenibacillus_F sp000411255 | |||||||||||
CAZyme ID | MGYG000001436_03505 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Validoxylamine A glucosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 672164; End: 673063 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 6 | 131 | 2.6e-22 | 0.7411764705882353 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06420 | GT2_Chondriotin_Pol_N | 1.12e-12 | 6 | 226 | 1 | 181 | 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. |
cd00761 | Glyco_tranf_GTA_type | 1.53e-08 | 6 | 117 | 1 | 112 | 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. |
COG1216 | GT2 | 2.12e-08 | 1 | 280 | 2 | 286 | Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]. |
pfam13641 | Glyco_tranf_2_3 | 1.27e-07 | 6 | 222 | 6 | 208 | Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis. |
COG1215 | BcsA | 8.68e-06 | 3 | 240 | 55 | 275 | Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QAV17295.1 | 2.10e-215 | 1 | 299 | 1 | 299 |
QKS43719.1 | 1.56e-105 | 4 | 294 | 5 | 297 |
ATL25034.1 | 1.07e-52 | 5 | 293 | 8 | 302 |
QTB15740.1 | 3.98e-36 | 3 | 242 | 2 | 245 |
AJQ26617.1 | 3.87e-34 | 5 | 282 | 22 | 300 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2Z87_A | 6.38e-14 | 4 | 229 | 94 | 332 | 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 | 6.39e-14 | 4 | 229 | 95 | 333 | 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 |
---|---|---|---|---|---|---|
H2K893 | 2.89e-24 | 4 | 251 | 11 | 267 | Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. jinggangensis (strain 5008) OX=1133850 GN=valG PE=1 SV=1 |
Q15JF5 | 4.62e-23 | 4 | 251 | 42 | 298 | Validoxylamine A glucosyltransferase OS=Streptomyces hygroscopicus subsp. limoneus OX=264445 GN=vldK PE=3 SV=1 |
O06483 | 3.92e-14 | 3 | 237 | 2 | 265 | Uncharacterized glycosyltransferase YfnE OS=Bacillus subtilis (strain 168) OX=224308 GN=yfnE PE=3 SV=2 |
Q8L0V4 | 3.64e-13 | 4 | 229 | 152 | 390 | Chondroitin synthase OS=Escherichia coli OX=562 GN=kfoC PE=1 SV=1 |
Q7BLV3 | 1.04e-11 | 4 | 210 | 160 | 379 | Hyaluronan synthase OS=Pasteurella multocida OX=747 GN=hyaD PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000066 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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