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CAZyme Information: MGYG000001523_03007

You are here: Home > Sequence: MGYG000001523_03007

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 Gracilibacillus massiliensis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Gracilibacillus; Gracilibacillus massiliensis
CAZyme ID MGYG000001523_03007
CAZy Family GT2
CAZyme Description Poly-beta-1,6-N-acetyl-D-glucosamine synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
461 MGYG000001523_13|CGC11 53217.92 9.8301
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001523 4207224 Isolate not provided not provided
Gene Location Start: 530565;  End: 531950  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001523_03007.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 44 244 2.1e-26 0.9705882352941176
GT2 148 368 1.4e-16 0.949238578680203

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06423 CESA_like 5.31e-52 45 257 1 180
CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
COG1215 BcsA 1.62e-40 1 421 13 401
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
PRK11204 PRK11204 1.21e-33 42 305 55 275
N-glycosyltransferase; Provisional
cd06439 CESA_like_1 1.17e-30 43 304 31 243
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily. This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.
cd04192 GT_2_like_e 1.82e-26 45 305 1 226
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
ADU29694.1 2.83e-181 38 461 38 457
QTM99193.1 2.16e-178 1 440 1 438
QED46831.1 1.20e-149 39 441 38 437
UAC49812.1 5.96e-145 38 449 38 446
QFK73069.1 2.21e-143 38 446 42 447

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5HEA_A 4.29e-08 43 159 7 98
CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213]
5EKE_A 3.02e-07 41 163 26 126
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKP_A 3.02e-07 41 163 26 126
Structureof the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]
6YV7_B 5.62e-07 43 319 44 271
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_A 5.64e-07 43 319 45 272
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GLC5 1.58e-21 42 308 48 270
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus epidermidis OX=1282 GN=icaA PE=3 SV=1
Q6GDD8 2.13e-21 42 308 48 270
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=icaA PE=3 SV=1
Q5HCN1 2.13e-21 42 308 48 270
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain COL) OX=93062 GN=icaA PE=3 SV=1
Q7A351 2.13e-21 42 308 48 270
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain N315) OX=158879 GN=icaA PE=3 SV=1
Q99QX3 2.13e-21 42 308 48 270
Poly-beta-1,6-N-acetyl-D-glucosamine synthase OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=icaA 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
0.998495 0.001526 0.000010 0.000003 0.000002 0.000008

TMHMM  Annotations      download full data without filtering help

start end
5 27
334 356
363 385
409 428