logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001451_04287

You are here: Home > Sequence: MGYG000001451_04287

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 Paenibacillus_A antibioticophila
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila
CAZyme ID MGYG000001451_04287
CAZy Family GT4
CAZyme Description Spore coat protein SA
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
383 MGYG000001451_4|CGC2 42575.06 10.1629
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001451 5573040 Isolate not provided not provided
Gene Location Start: 124433;  End: 125584  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001451_04287.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT4 195 354 8.4e-40 0.94375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03801 GT4_PimA-like 5.18e-63 5 378 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.
pfam00534 Glycos_transf_1 1.85e-45 195 359 1 157
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.
COG0438 RfaB 6.84e-43 5 380 2 376
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03800 GT4_sucrose_synthase 1.22e-38 184 373 207 395
sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
pfam13692 Glyco_trans_1_4 1.95e-36 196 346 1 138
Glycosyl transferases group 1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANS77253.1 8.06e-160 1 379 11 389
AWB45820.1 7.72e-154 1 377 1 377
AZS18439.1 9.09e-149 1 374 1 374
ANY72476.1 3.85e-145 1 377 1 377
AYB45887.1 5.11e-143 1 380 1 380

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6TVP_A 9.45e-22 132 383 151 401
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]
3C4Q_A 2.01e-19 136 379 166 403
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 2.16e-19 136 379 186 423
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]
3OKA_A 2.44e-17 107 381 112 379
Crystalstructure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum]
3OKC_A 2.67e-17 107 381 112 379
Crystalstructure of Corynebacterium glutamicum PimB' bound to GDP (orthorhombic crystal form) [Corynebacterium glutamicum],3OKP_A Crystal structure of Corynebacterium glutamicum PimB' bound to GDP-Man (orthorhombic crystal form) [Corynebacterium glutamicum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P46915 9.35e-59 5 382 2 377
Spore coat protein SA OS=Bacillus subtilis (strain 168) OX=224308 GN=cotSA PE=1 SV=1
O34413 2.14e-52 5 380 2 375
Putative glycosyltransferase YtcC OS=Bacillus subtilis (strain 168) OX=224308 GN=ytcC PE=3 SV=1
D5UJ42 5.45e-23 136 379 201 437
D-inositol 3-phosphate glycosyltransferase OS=Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 / NCIMB 8073 / NRS 134) OX=446466 GN=mshA PE=3 SV=1
P26470 3.12e-21 74 374 90 371
Lipopolysaccharide 1,2-N-acetylglucosaminetransferase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=waaK PE=3 SV=1
D1BD84 3.31e-21 136 378 172 414
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

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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001451_04287.