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CAZyme Information: MGYG000000367_00103

You are here: Home > Sequence: MGYG000000367_00103

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 QAKD01 sp003343965
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; QAKD01; QAKD01 sp003343965
CAZyme ID MGYG000000367_00103
CAZy Family GT4
CAZyme Description Putative glycosyltransferase EpsD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
375 MGYG000000367_2|CGC1 41856.51 9.5801
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000367 1764233 MAG Sweden Europe
Gene Location Start: 9144;  End: 10271  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000367_00103.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 199 343 2.2e-34 0.91875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03808 GT4_CapM-like 7.17e-80 3 367 1 357
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.
cd03801 GT4_PimA-like 1.45e-54 22 372 24 366
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.
cd03817 GT4_UGDG-like 3.37e-42 21 374 23 372
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
cd03807 GT4_WbnK-like 2.73e-40 75 372 71 362
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.
COG0438 RfaB 2.34e-38 1 375 1 378
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
APM40301.1 4.88e-117 1 371 1 367
QXJ38641.1 1.84e-116 2 375 3 372
AMC92674.1 8.17e-116 1 373 1 371
ALG41879.1 1.73e-112 1 371 1 372
QCR31886.1 1.38e-109 1 375 1 377

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3C4Q_A 2.36e-16 137 375 158 406
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 2.48e-16 137 375 178 426
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]
6EJI_A 6.63e-14 203 366 185 349
Structureof a glycosyltransferase [Campylobacter jejuni],6EJI_B Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_A Structure of a glycosyltransferase [Campylobacter jejuni],6EJK_B Structure of a glycosyltransferase [Campylobacter jejuni]
6EJJ_A 6.63e-14 203 366 185 349
Structureof a glycosyltransferase / state 2 [Campylobacter jejuni],6EJJ_B Structure of a glycosyltransferase / state 2 [Campylobacter jejuni]
6TVP_A 1.36e-13 55 373 65 398
Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P71053 1.48e-97 2 374 3 371
Putative glycosyltransferase EpsD OS=Bacillus subtilis (strain 168) OX=224308 GN=epsD PE=2 SV=1
P71055 3.42e-20 73 304 77 309
Putative glycosyltransferase EpsF OS=Bacillus subtilis (strain 168) OX=224308 GN=epsF PE=2 SV=1
D1BD84 1.30e-18 84 373 109 416
D-inositol 3-phosphate glycosyltransferase OS=Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74) OX=446469 GN=mshA PE=3 SV=1
C4LLD6 1.55e-18 81 375 128 435
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
P39862 1.48e-17 22 340 23 338
Capsular polysaccharide biosynthesis glycosyltransferase CapM OS=Staphylococcus aureus OX=1280 GN=capM 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
0.999893 0.000137 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000367_00103.