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CAZyme Information: MGYG000001831_00929

You are here: Home > Sequence: MGYG000001831_00929

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 TF01-11 sp000436755
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp000436755
CAZyme ID MGYG000001831_00929
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
315 36443.94 9.4293
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001831 3856267 MAG Denmark Europe
Gene Location Start: 34538;  End: 35485  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001831_00929.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 3 113 1.7e-21 0.6352941176470588

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04196 GT_2_like_d 9.15e-86 3 225 1 214
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.
cd00761 Glyco_tranf_GTA_type 1.34e-21 4 113 1 107
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 1.67e-19 3 173 1 163
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.
COG0463 WcaA 7.84e-15 1 314 4 291
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd02525 Succinoglycan_BP_ExoA 2.14e-12 2 110 2 108
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL39274.1 3.52e-91 1 315 1 311
AQP38863.1 7.06e-91 1 315 1 311
QCP36319.1 4.60e-89 1 315 1 311
QMW70493.1 6.51e-89 1 315 1 311
BCD36647.1 6.51e-89 1 315 1 311

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3L7I_A 1.71e-08 2 94 4 94
Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A]
3L7J_A 1.71e-08 2 94 4 94
ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A]
3L7M_A 1.71e-08 2 94 4 94
ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A]
5HEA_A 3.77e-08 1 110 6 111
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]
1H7L_A 1.82e-06 2 101 3 106
dTDP-MAGNESIUMCOMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1H7Q_A dTDP-MANGANESE COMPLEX OF SPSA FROM BACILLUS SUBTILIS [Bacillus subtilis],1QG8_A Native (Magnesium-Containing) Spsa From Bacillus Subtilis [Bacillus subtilis],1QGQ_A Udp-manganese Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis],1QGS_A Udp-Magnesium Complex Of Spsa From Bacillus Subtilis [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P37783 1.03e-19 6 243 1 231
dTDP-rhamnosyl transferase RfbG OS=Shigella flexneri OX=623 GN=rfbG PE=3 SV=1
O32268 1.11e-12 1 110 7 113
Putative teichuronic acid biosynthesis glycosyltransferase TuaG OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaG PE=2 SV=1
Q57022 8.02e-11 1 135 5 129
Uncharacterized glycosyltransferase HI_0868 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0868 PE=3 SV=1
P22639 1.97e-10 2 220 3 214
Uncharacterized glycosyltransferase alr2836 OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=alr2836 PE=3 SV=2
Q57287 4.83e-10 1 313 6 296
Uncharacterized glycosyltransferase HI_1578 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1578 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
1.000033 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001831_00929.