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CAZyme Information: MGYG000001624_00786

You are here: Home > Sequence: MGYG000001624_00786

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 Proteus cibarius
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Proteus; Proteus cibarius
CAZyme ID MGYG000001624_00786
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
375 41881.44 9.7637
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001624 3841359 MAG China Asia
Gene Location Start: 597;  End: 1724  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001624_00786.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 189 341 4.4e-37 0.95625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 1.14e-75 8 364 4 365
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.
cd03807 GT4_WbnK-like 6.23e-61 18 361 12 358
Shigella dysenteriae WbnK and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
cd03808 GT4_CapM-like 3.26e-53 29 361 21 358
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
COG0438 RfaB 2.98e-49 1 371 1 381
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03798 GT4_WlbH-like 7.42e-48 18 364 14 373
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ATM98912.1 1.10e-278 1 375 1 375
QHD94142.1 5.22e-277 1 375 1 375
QUT01891.1 5.22e-277 1 375 1 375
QJW49406.1 5.22e-277 1 375 1 375
QKD72921.1 1.50e-276 1 375 1 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5I45_A 1.35e-23 168 371 5 216
1.35Angstrom Crystal Structure of C-terminal Domain of Glycosyl Transferase Group 1 Family Protein (LpcC) from Francisella tularensis. [Francisella tularensis subsp. tularensis SCHU S4]
3C4Q_A 3.55e-21 141 347 170 386
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 3.86e-21 141 347 190 406
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]
2JJM_A 3.62e-19 134 375 154 394
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 4.18e-19 134 375 174 414
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8NTA6 1.83e-20 141 347 170 386
D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mshA PE=1 SV=1
A4QB40 1.83e-20 141 347 170 386
D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium glutamicum (strain R) OX=340322 GN=mshA PE=3 SV=1
D3Q051 5.43e-20 18 368 43 428
D-inositol 3-phosphate glycosyltransferase OS=Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 / LLR-40K-21) OX=446470 GN=mshA PE=3 SV=1
O05083 1.01e-18 18 339 15 329
Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 PE=3 SV=1
B1VEI4 1.34e-18 51 364 70 403
D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109) OX=504474 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
1.000063 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001624_00786.