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CAZyme Information: MGYG000001741_01337

You are here: Home > Sequence: MGYG000001741_01337

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 Collinsella sp900549555
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900549555
CAZyme ID MGYG000001741_01337
CAZy Family GT4
CAZyme Description D-inositol-3-phosphate glycosyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
360 MGYG000001741_29|CGC1 39365.31 6.7675
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001741 2087019 MAG Sweden Europe
Gene Location Start: 24492;  End: 25574  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001741_01337.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 183 329 2.1e-36 0.91875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 6.52e-59 11 353 1 365
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.
COG0438 RfaB 4.88e-48 62 360 70 381
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03808 GT4_CapM-like 5.08e-48 64 350 68 358
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.
pfam00534 Glycos_transf_1 3.94e-42 183 335 5 158
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.
cd03820 GT4_AmsD-like 6.83e-39 137 336 139 337
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ABG85816.1 4.94e-74 11 353 3 344
QXX09143.1 1.17e-65 13 353 7 352
QKH83075.1 4.68e-63 11 355 3 342
QRQ47357.1 9.84e-63 11 353 5 342
ANW26304.1 1.90e-62 13 353 14 359

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4N9W_A 8.24e-18 177 353 189 364
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 9.14e-18 177 353 205 380
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 2.50e-17 75 329 102 379
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 2.65e-17 75 329 122 399
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]
6EJJ_A 5.83e-14 183 348 186 349
Structureof a glycosyltransferase / state 2 [Campylobacter jejuni],6EJJ_B Structure of a glycosyltransferase / state 2 [Campylobacter jejuni]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B1VS68 1.28e-19 184 358 278 461
D-inositol 3-phosphate glycosyltransferase OS=Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350) OX=455632 GN=mshA PE=3 SV=1
C3PK12 3.64e-18 177 358 220 407
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
Q6NJL3 3.77e-18 177 332 223 385
D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) OX=257309 GN=mshA PE=3 SV=1
O05083 2.47e-17 138 352 139 352
Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 PE=3 SV=1
D7C367 2.61e-17 137 330 202 418
D-inositol 3-phosphate glycosyltransferase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 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
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001741_01337.