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CAZyme Information: MGYG000003322_01356

You are here: Home > Sequence: MGYG000003322_01356

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
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella;
CAZyme ID MGYG000003322_01356
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
150 16123.38 4.5234
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003322 1648873 MAG United Republic of Tanzania Africa
Gene Location Start: 2715;  End: 3167  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003322_01356.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 3 117 7.6e-17 0.75

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0438 RfaB 1.82e-20 2 150 223 380
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03801 GT4_PimA-like 2.48e-20 2 124 216 343
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.
cd03823 GT4_ExpE7-like 1.84e-19 6 144 217 355
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).
cd03814 GT4-like 2.28e-19 1 145 220 365
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.
pfam00534 Glycos_transf_1 5.74e-19 3 124 27 154
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK90017.1 3.91e-36 1 149 256 397
AMK55395.1 6.39e-36 1 144 210 353
QMW78049.1 8.17e-35 1 149 255 403
QIB53531.1 8.17e-35 1 149 255 403
QRT49764.1 1.07e-34 1 144 255 398

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2JJM_A 9.91e-07 59 116 295 352
CrystalStructure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames]
3MBO_A 1.00e-06 59 116 315 372
CrystalStructure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_B Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_C Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_D Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_E Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_F Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_G Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_H Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis]
3C4Q_A 6.34e-06 41 116 299 373
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 6.38e-06 41 116 319 393
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
Q8S4F6 3.58e-11 1 114 323 445
Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 SV=1
C4LLD6 6.44e-11 3 150 276 437
D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717) OX=645127 GN=mshA PE=3 SV=1
C7MSY6 8.82e-07 38 148 309 419
D-inositol 3-phosphate glycosyltransferase OS=Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101) OX=471857 GN=mshA PE=3 SV=1
C3PK12 1.19e-06 39 148 297 406
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
A4FQ08 2.22e-06 38 147 309 418
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

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
1.000076 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003322_01356.