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CAZyme Information: MGYG000001370_02880

You are here: Home > Sequence: MGYG000001370_02880

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 Bacteroides fluxus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides fluxus
CAZyme ID MGYG000001370_02880
CAZy Family GT27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
556 MGYG000001370_88|CGC2 64218.11 6.2934
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001370 4330086 Isolate not provided not provided
Gene Location Start: 62803;  End: 64473  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001370_02880.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT27 9 309 5e-34 0.9796610169491525

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02510 pp-GalNAc-T 1.74e-08 8 239 1 234
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.
pfam00535 Glycos_transf_2 1.75e-08 8 161 1 153
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.
cd00761 Glyco_tranf_GTA_type 6.17e-07 9 118 1 112
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.
cd04793 LanC 1.53e-04 349 478 1 137
Cyclases involved in the biosynthesis of lantibiotics. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthinoine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as precursor peptides and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans) in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. Also contains SpaC (the cyclase involved in the biosynthesis of subtilin), NisC, and homologs.
cd04186 GT_2_like_c 3.70e-04 9 114 1 105
Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIK61404.1 1.23e-112 6 520 11 519
QIU94695.1 7.38e-63 3 265 1 254
QUB82074.1 4.91e-60 1 268 1 260
ALZ75925.1 5.31e-51 8 265 5 255
BAR48611.1 2.01e-33 5 148 9 150

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2D7I_A 5.10e-16 8 239 115 346
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]
6S22_A 8.67e-10 8 307 186 484
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]
6E4R_A 9.09e-09 6 239 70 306
CrystalStructure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9B [Drosophila melanogaster],6E4R_B Crystal Structure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9B [Drosophila melanogaster]
6E4Q_A 9.13e-09 6 239 70 306
CrystalStructure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9A in Complex with UDP and Mn2+ [Drosophila melanogaster],6E4Q_B Crystal Structure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9A in Complex with UDP and Mn2+ [Drosophila melanogaster],6E4Q_C Crystal Structure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9A in Complex with UDP and Mn2+ [Drosophila melanogaster],6E4Q_D Crystal Structure of the Drosophila Melanogaster Polypeptide N-Acetylgalactosaminyl Transferase PGANT9A in Complex with UDP and Mn2+ [Drosophila melanogaster]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q86SR1 2.98e-15 8 239 148 379
Polypeptide N-acetylgalactosaminyltransferase 10 OS=Homo sapiens OX=9606 GN=GALNT10 PE=1 SV=2
Q925R7 5.23e-15 8 239 148 379
Polypeptide N-acetylgalactosaminyltransferase 10 OS=Rattus norvegicus OX=10116 GN=Galnt10 PE=2 SV=1
Q6P9S7 6.93e-15 8 239 148 379
Polypeptide N-acetylgalactosaminyltransferase 10 OS=Mus musculus OX=10090 GN=Galnt10 PE=2 SV=1
Q96FL9 3.03e-12 8 238 114 341
Polypeptide N-acetylgalactosaminyltransferase 14 OS=Homo sapiens OX=9606 GN=GALNT14 PE=1 SV=1
Q7K755 1.01e-11 8 238 162 396
Putative polypeptide N-acetylgalactosaminyltransferase 11 OS=Caenorhabditis elegans OX=6239 GN=gly-11 PE=3 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001370_02880.