logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001848_00852

You are here: Home > Sequence: MGYG000001848_00852

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 Eubacterium_F sp000433735
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_F; Eubacterium_F sp000433735
CAZyme ID MGYG000001848_00852
CAZy Family GT2
CAZyme Description Teichoic acid poly(glycerol phosphate) polymerase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
719 MGYG000001848_3|CGC1 84674.53 5.898
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001848 2356822 MAG Denmark Europe
Gene Location Start: 19857;  End: 22016  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001848_00852.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 5 140 5.1e-19 0.7941176470588235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam04464 Glyphos_transf 4.07e-127 352 717 1 360
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase. Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.
COG1887 TagB 6.28e-90 346 719 17 388
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism].
pfam00535 Glycos_transf_2 1.81e-17 5 170 1 164
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 4.87e-16 6 155 1 149
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.
COG0463 WcaA 4.00e-12 1 103 2 108
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCD36649.1 1.30e-183 3 717 2 711
QMW70491.1 3.05e-183 3 717 29 738
QSI24418.1 1.13e-181 1 716 1 746
BCL57396.1 1.74e-180 3 717 2 743
CUH93481.1 2.05e-179 3 719 2 778

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3L7I_A 1.46e-112 1 709 1 708
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 1.56e-111 1 709 1 708
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 4.31e-111 1 709 1 708
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]
3BCV_A 2.86e-07 3 218 6 229
Crystalstructure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343]
5TZE_C 6.09e-06 3 95 2 101
Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5HLM5 6.53e-112 1 709 1 708
Teichoic acid poly(glycerol phosphate) polymerase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=tagF PE=1 SV=1
P13485 7.53e-103 350 719 376 746
Teichoic acid poly(glycerol phosphate) polymerase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagF PE=1 SV=1
Q2G1C1 4.24e-96 341 717 8 389
Teichoic acid glycerol-phosphate transferase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=tarF PE=1 SV=1
Q8RKI5 1.14e-93 351 715 27 392
Teichoic acid poly(glycerol phosphate) polymerase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarF PE=1 SV=1
Q2G1C2 4.90e-25 439 718 241 513
Teichoic acid ribitol-phosphate polymerase TarK OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=tarK PE=1 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
1.000051 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001848_00852.