Species | Rothia aeria | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia aeria | |||||||||||
CAZyme ID | MGYG000003000_00799 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 4182; End: 5363 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03804 | GT4_WbaZ-like | 4.34e-95 | 31 | 381 | 2 | 351 | mannosyltransferase WbaZ and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity. |
cd03801 | GT4_PimA-like | 6.62e-28 | 33 | 387 | 5 | 363 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. The members of this family are found mainly in certain bacteria and archaea. |
COG0438 | RfaB | 6.51e-25 | 31 | 392 | 3 | 377 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
pfam00534 | Glycos_transf_1 | 7.29e-23 | 233 | 359 | 4 | 141 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
cd03805 | GT4_ALG2-like | 5.31e-20 | 42 | 385 | 13 | 392 | alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QXW92863.1 | 1.27e-293 | 1 | 393 | 1 | 393 |
VEI22477.1 | 2.56e-293 | 1 | 393 | 1 | 393 |
BAV87417.1 | 1.00e-290 | 1 | 393 | 1 | 393 |
QQT89702.1 | 1.00e-290 | 1 | 393 | 1 | 393 |
BAI65409.1 | 5.33e-192 | 14 | 392 | 34 | 412 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2F9F_A | 1.07e-20 | 226 | 354 | 18 | 155 | CrystalStructure of the Putative Mannosyl Transferase (wbaZ-1)from Archaeoglobus fulgidus, Northeast Structural Genomics Target GR29A. [Archaeoglobus fulgidus DSM 4304] |
3C4Q_A | 6.69e-07 | 237 | 358 | 229 | 367 | Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum] |
3C48_A | 6.83e-07 | 237 | 358 | 249 | 387 | Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum] |
2R60_A | 4.03e-06 | 292 | 384 | 351 | 446 | Structureof apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii [Halothermothrix orenii],2R66_A Complex Structure of Sucrose Phosphate Synthase (SPS)-F6P of Halothermothrix orenii [Halothermothrix orenii H 168],2R68_A Complex Structure of Sucrose Phosphate Synthase (SPS)-S6P of Halothermothrix orenii [Halothermothrix orenii H 168] |
5ZE7_A | 4.15e-06 | 237 | 381 | 191 | 335 | UDPGlucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZE7_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - apo form [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_A UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZES_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP complex [Synechococcus elongatus PCC 7942 = FACHB-805],5ZFK_B UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC 7942 - UDP-BH2 complex [Synechococcus elongatus PCC 7942 = FACHB-805] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9H553 | 6.86e-09 | 224 | 392 | 216 | 414 | Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Homo sapiens OX=9606 GN=ALG2 PE=1 SV=1 |
Q7KWM5 | 2.17e-08 | 230 | 392 | 226 | 420 | Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Dictyostelium discoideum OX=44689 GN=alg2 PE=3 SV=1 |
P13484 | 3.95e-08 | 192 | 381 | 313 | 500 | Poly(glycerol-phosphate) alpha-glucosyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagE PE=1 SV=1 |
A0R043 | 8.19e-08 | 31 | 356 | 2 | 335 | GDP-mannose-dependent alpha-(1-6)-phosphatidylinositol monomannoside mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=pimB PE=1 SV=1 |
A0QRG8 | 1.07e-07 | 237 | 345 | 209 | 317 | GDP-mannose-dependent alpha-mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mgtA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000048 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.