Species | Corynebacterium ammoniagenes | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium ammoniagenes | |||||||||||
CAZyme ID | MGYG000001533_01871 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | GDP-mannose-dependent alpha-mannosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2002592; End: 2003716 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03814 | GT4-like | 1.16e-112 | 2 | 370 | 1 | 365 | glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 bacteria and eukaryotes. |
PLN02871 | PLN02871 | 3.28e-102 | 2 | 373 | 60 | 436 | UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
cd03817 | GT4_UGDG-like | 2.97e-67 | 2 | 369 | 1 | 372 | UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol. |
cd03801 | GT4_PimA-like | 2.01e-63 | 2 | 370 | 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 | 1.07e-58 | 1 | 374 | 1 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AQS74117.1 | 2.05e-278 | 1 | 374 | 1 | 374 |
APT83086.1 | 2.05e-278 | 1 | 374 | 1 | 374 |
AQX71494.1 | 2.95e-246 | 1 | 374 | 1 | 374 |
AMJ45044.1 | 2.95e-246 | 1 | 374 | 1 | 374 |
ASJ19178.1 | 2.95e-246 | 1 | 374 | 1 | 374 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4N9W_A | 3.47e-19 | 1 | 374 | 5 | 369 | Crystalstructure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155] |
2GEJ_A | 3.91e-19 | 1 | 374 | 21 | 385 | CrystalStructure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155] |
6TVP_A | 2.06e-16 | 1 | 371 | 15 | 398 | 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] |
3C4Q_A | 1.37e-15 | 165 | 373 | 188 | 406 | 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 | 1.44e-15 | 165 | 373 | 208 | 426 | 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 |
---|---|---|---|---|---|---|
Q8S4F6 | 6.14e-63 | 14 | 362 | 118 | 469 | Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 SV=1 |
A0QRG8 | 1.02e-53 | 1 | 374 | 1 | 368 | GDP-mannose-dependent alpha-mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mgtA PE=3 SV=1 |
P9WMY4 | 3.25e-52 | 1 | 374 | 4 | 371 | GDP-mannose-dependent alpha-mannosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=mgtA PE=3 SV=1 |
P9WMY5 | 3.25e-52 | 1 | 374 | 4 | 371 | GDP-mannose-dependent alpha-mannosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=mgtA PE=1 SV=1 |
Q8NT41 | 4.46e-49 | 1 | 373 | 7 | 375 | GDP-mannose-dependent alpha-mannosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mgtA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000034 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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