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CAZyme Information: MGYG000000600_00501

You are here: Home > Sequence: MGYG000000600_00501

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 CAG-791 sp000431495
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-791; CAG-791 sp000431495
CAZyme ID MGYG000000600_00501
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
426 48025.19 6.388
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000600 2612842 MAG Madagascar Africa
Gene Location Start: 16686;  End: 17966  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000600_00501.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 237 395 2.7e-28 0.85625

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 1.40e-32 210 422 175 366
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 5.63e-27 82 426 71 379
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534 Glycos_transf_1 9.88e-26 237 402 13 157
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.
pfam13692 Glyco_trans_1_4 4.01e-25 229 389 5 138
Glycosyl transferases group 1.
cd03798 GT4_WlbH-like 3.84e-22 236 424 210 376
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL35301.1 9.86e-158 1 424 10 424
AOZ97462.1 8.33e-154 1 424 12 422
QNM02200.1 4.10e-105 1 369 10 378
QEL87780.1 5.15e-98 4 424 16 418
QGV06202.1 1.03e-97 4 424 16 418

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4XSO_A 3.06e-07 237 424 217 384
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]
4N9W_A 1.27e-06 229 424 196 367
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 1.31e-06 229 424 212 383
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]
3C4Q_A 9.81e-06 170 404 169 386
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 1.00e-05 170 404 189 406
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q46638 6.17e-12 286 424 259 406
Amylovoran biosynthesis glycosyltransferase AmsK OS=Erwinia amylovora OX=552 GN=amsK PE=3 SV=2
O34413 4.39e-08 223 424 187 376
Putative glycosyltransferase YtcC OS=Bacillus subtilis (strain 168) OX=224308 GN=ytcC PE=3 SV=1
P46915 5.34e-08 238 404 203 356
Spore coat protein SA OS=Bacillus subtilis (strain 168) OX=224308 GN=cotSA PE=1 SV=1
P26388 7.73e-08 284 380 259 361
Putative colanic acid biosynthesis glycosyltransferase WcaL OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=wcaL PE=3 SV=1
A1SP12 1.52e-07 237 422 270 448
D-inositol 3-phosphate glycosyltransferase OS=Nocardioides sp. (strain ATCC BAA-499 / JS614) OX=196162 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
1.000062 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000600_00501.