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CAZyme Information: MGYG000004754_01670

You are here: Home > Sequence: MGYG000004754_01670

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 Elizabethkingia bruuniana
Lineage Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Elizabethkingia; Elizabethkingia bruuniana
CAZyme ID MGYG000004754_01670
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
486 56763.13 7.1827
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004754 4072783 MAG China Asia
Gene Location Start: 734561;  End: 736021  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004754_01670.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02511 Beta4Glucosyltransferase 2.02e-10 306 448 23 147
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.
TIGR04195 S_glycosyl_SunS 4.48e-07 273 446 53 201
peptide S-glycosyltransferase, SunS family. Members of this family include SunS, the S-glycosyltransferase that transfers a sugar (substrate is variable in reconstitution assays) onto the precursor of the glycopeptide sublancin, which once was thought to be a lantibiotic.
cd00761 Glyco_tranf_GTA_type 1.53e-05 286 392 3 110
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.
pfam00535 Glycos_transf_2 2.31e-05 286 416 4 136
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQN59960.1 0.0 1 486 1 486
ATL44754.1 0.0 1 486 1 486
AJW63804.1 0.0 1 486 1 486
QRI48595.1 4.48e-302 1 485 1 484
AQX09077.1 2.20e-294 15 485 1 470

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004754_01670.