Species | Muribaculum sp002358615 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Muribaculum; Muribaculum sp002358615 | |||||||||||
CAZyme ID | MGYG000000056_00896 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 97254; End: 98516 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03825 | GT4_WcaC-like | 9.05e-141 | 1 | 415 | 1 | 364 | putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis. |
cd03801 | GT4_PimA-like | 8.07e-51 | 2 | 413 | 1 | 366 | 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 | 8.22e-41 | 1 | 419 | 3 | 381 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03798 | GT4_WlbH-like | 4.64e-31 | 3 | 415 | 1 | 376 | Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS. |
cd03823 | GT4_ExpE7-like | 8.65e-29 | 2 | 414 | 1 | 357 | glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II). |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ALB75738.1 | 7.96e-188 | 1 | 419 | 1 | 419 |
QRO24366.1 | 1.91e-181 | 1 | 415 | 1 | 415 |
ADY36895.1 | 5.96e-178 | 1 | 415 | 1 | 415 |
QUT60038.1 | 1.70e-177 | 1 | 415 | 1 | 415 |
QQY42003.1 | 2.41e-177 | 1 | 415 | 1 | 415 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6TVP_A | 4.23e-08 | 212 | 367 | 183 | 344 | Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155] |
5D00_A | 9.34e-08 | 13 | 362 | 17 | 321 | Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168] |
4XSO_A | 1.69e-07 | 200 | 408 | 171 | 368 | ChainA, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSO_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418] |
3C4Q_A | 2.45e-07 | 100 | 379 | 104 | 369 | 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 | 2.50e-07 | 100 | 379 | 124 | 389 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D7AW65 | 3.35e-16 | 100 | 376 | 116 | 378 | D-inositol 3-phosphate glycosyltransferase OS=Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509) OX=446468 GN=mshA PE=3 SV=1 |
C3PK12 | 2.50e-15 | 13 | 401 | 22 | 387 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1) OX=548476 GN=mshA PE=3 SV=1 |
C7Q4Y6 | 5.92e-15 | 93 | 420 | 102 | 415 | D-inositol 3-phosphate glycosyltransferase 1 OS=Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908) OX=479433 GN=mshA1 PE=3 SV=1 |
A4FQ08 | 1.52e-14 | 209 | 360 | 203 | 363 | D-inositol 3-phosphate glycosyltransferase OS=Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338) OX=405948 GN=mshA PE=3 SV=1 |
D2S4K7 | 1.64e-13 | 182 | 379 | 170 | 382 | D-inositol 3-phosphate glycosyltransferase OS=Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20) OX=526225 GN=mshA PE=3 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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