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CAZyme Information: MGYG000001262_03180

You are here: Home > Sequence: MGYG000001262_03180

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Sphingomonas ginsenosidimutans
Lineage Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; Sphingomonadaceae; Sphingomonas; Sphingomonas ginsenosidimutans
CAZyme ID MGYG000001262_03180
CAZy Family GT4
CAZyme Description D-inositol 3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
126 MGYG000001262_209|CGC1 13081.82 6.6013
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001262 3667136 MAG Italy Europe
Gene Location Start: 46;  End: 426  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001262_03180.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 2 92 8.5e-20 0.56875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 4.97e-22 2 104 247 355
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.
pfam00534 Glycos_transf_1 2.91e-21 3 93 59 150
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.
cd03811 GT4_GT28_WabH-like 8.92e-21 2 100 244 340
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
COG0438 RfaB 3.03e-20 3 104 257 364
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam13692 Glyco_trans_1_4 7.76e-20 2 87 55 138
Glycosyl transferases group 1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNE33388.1 1.98e-44 1 118 269 386
QKS01003.1 2.11e-43 1 125 265 389
QNA82647.1 1.13e-41 2 118 270 386
AMK19189.1 1.38e-40 4 117 273 386
QHD65645.1 5.28e-40 4 117 273 386

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6KIH_A 4.59e-08 1 88 302 390
Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus]
3C4Q_A 7.35e-07 4 110 287 398
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 7.38e-07 4 110 307 418
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C9ZH13 1.32e-14 1 122 311 437
D-inositol 3-phosphate glycosyltransferase OS=Streptomyces scabiei (strain 87.22) OX=680198 GN=mshA PE=3 SV=1
Q9FCG5 4.62e-14 1 108 323 435
D-inositol 3-phosphate glycosyltransferase OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=mshA PE=2 SV=2
C7QKE8 5.43e-13 1 109 290 403
D-inositol 3-phosphate glycosyltransferase 2 OS=Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908) OX=479433 GN=mshA2 PE=3 SV=1
D6Y4U7 5.44e-13 1 110 293 407
D-inositol 3-phosphate glycosyltransferase OS=Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 / NBRC 14880 / R51) OX=469371 GN=mshA PE=3 SV=1
D2B9F4 5.47e-13 1 122 301 428
D-inositol 3-phosphate glycosyltransferase OS=Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) OX=479432 GN=mshA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000035 0.000008 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001262_03180.