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CAZyme Information: MGYG000001514_04297

You are here: Home > Sequence: MGYG000001514_04297

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 ihumii
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A ihumii
CAZyme ID MGYG000001514_04297
CAZy Family GT27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
292 33041.62 4.5871
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001514 5923787 Isolate not provided not provided
Gene Location Start: 3078619;  End: 3079497  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001514_04297.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT27 9 219 1e-26 0.7796610169491526

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00535 Glycos_transf_2 3.47e-13 9 167 1 160
Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
cd02525 Succinoglycan_BP_ExoA 4.07e-12 7 226 1 222
ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.
cd02510 pp-GalNAc-T 2.21e-09 9 198 1 211
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans. UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.
PRK10073 PRK10073 3.52e-09 1 117 2 119
putative glycosyl transferase; Provisional
cd00761 Glyco_tranf_GTA_type 5.03e-07 10 118 1 113
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AZK48091.1 6.50e-156 1 292 1 292
QNF28463.1 8.90e-42 1 290 1 290
AGK52774.1 9.35e-42 7 290 9 292
ASS96799.1 4.06e-40 7 290 9 293
SQI61474.1 2.06e-39 1 290 1 290

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6S22_A 5.48e-07 9 218 186 420
Crystalstructure of the TgGalNAc-T3 in complex with UDP, manganese and FGF23c [Taeniopygia guttata],6S24_A Crystal structure of the TgGalNAc-T3 in complex with UDP, manganese and the peptide 3 [Taeniopygia guttata]
2D7I_A 9.34e-06 9 218 115 344
Crystalstructure of pp-GalNAc-T10 with UDP, GalNAc and Mn2+ [Homo sapiens],2D7R_A Crystal structure of pp-GalNAc-T10 complexed with GalNAc-Ser on lectin domain [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9VUT6 1.96e-15 8 214 130 353
Polypeptide N-acetylgalactosaminyltransferase 8 OS=Drosophila melanogaster OX=7227 GN=Pgant8 PE=1 SV=1
Q6DJR8 3.86e-08 7 272 145 425
Polypeptide N-acetylgalactosaminyltransferase 11 OS=Xenopus tropicalis OX=8364 GN=galnt11 PE=1 SV=2
Q7Z4T8 7.90e-08 38 205 168 354
Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 OS=Homo sapiens OX=9606 GN=GALNTL5 PE=2 SV=3
Q8MVS5 2.99e-07 38 221 182 389
Polypeptide N-acetylgalactosaminyltransferase 35A OS=Drosophila melanogaster OX=7227 GN=Pgant35A PE=1 SV=2
Q95JX4 3.38e-07 38 205 168 354
Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 OS=Macaca fascicularis OX=9541 GN=GALNTL5 PE=2 SV=2

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
1.000049 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001514_04297.