Species | Acidovorax temperans | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Acidovorax; Acidovorax temperans | |||||||||||
CAZyme ID | MGYG000001264_01893 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36; End: 2366 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 527 | 695 | 8.6e-33 | 0.9705882352941176 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04950 | GT4_TuaH-like | 2.67e-70 | 154 | 518 | 2 | 369 | teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
cd04186 | GT_2_like_c | 1.85e-47 | 528 | 737 | 1 | 165 | 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. |
COG1216 | GT2 | 1.03e-41 | 523 | 772 | 2 | 255 | Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism]. |
pfam00535 | Glycos_transf_2 | 4.28e-31 | 527 | 695 | 1 | 164 | 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 | 1.01e-29 | 528 | 644 | 1 | 116 | 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 |
---|---|---|---|---|---|
AVZ37440.1 | 0.0 | 65 | 775 | 472 | 1182 |
QKV51754.1 | 0.0 | 69 | 774 | 304 | 1009 |
QRX81009.1 | 4.96e-318 | 67 | 774 | 309 | 1015 |
QBP73984.1 | 2.16e-298 | 67 | 773 | 270 | 975 |
AKJ98229.1 | 8.65e-272 | 67 | 775 | 105 | 815 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6YV7_B | 1.31e-14 | 524 | 732 | 42 | 242 | 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 | 1.32e-14 | 524 | 732 | 43 | 243 | 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] |
5HEA_A | 3.70e-09 | 526 | 628 | 7 | 107 | 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] |
6P61_A | 5.74e-09 | 522 | 639 | 11 | 126 | Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197] |
2Z86_A | 1.01e-08 | 522 | 652 | 373 | 501 | 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 |
---|---|---|---|---|---|---|
O32267 | 2.25e-18 | 278 | 507 | 130 | 380 | Putative teichuronic acid biosynthesis glycosyltransferase TuaH OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaH PE=2 SV=1 |
P55465 | 1.44e-14 | 524 | 765 | 625 | 874 | Uncharacterized protein y4gI OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=NGR_a03550 PE=4 SV=1 |
Q57287 | 5.74e-11 | 524 | 640 | 5 | 120 | Uncharacterized glycosyltransferase HI_1578 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1578 PE=3 SV=1 |
A0A0H2UR96 | 2.00e-10 | 526 | 741 | 5 | 220 | Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1 |
D4GYG7 | 4.95e-10 | 523 | 736 | 5 | 208 | Glycosyltransferase AglE OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglE PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000049 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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