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CAZyme Information: MGYG000001302.1_01418

You are here: Home > Sequence: MGYG000001302.1_01418

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 Alistipes putredinis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes putredinis
CAZyme ID MGYG000001302.1_01418
CAZy Family GT27
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
330 MGYG000001302.1_5|CGC1 36744.2 8.9448
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001302.1 2548229 Isolate not provided not provided
Gene Location Start: 177371;  End: 178363  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001302.1_01418.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT27 9 234 3.2e-20 0.7796610169491526

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04186 GT_2_like_c 3.14e-49 2 216 3 166
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.
COG1216 GT2 3.94e-49 2 306 9 304
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd00761 Glyco_tranf_GTA_type 6.29e-18 2 124 3 128
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.
cd02526 GT2_RfbF_like 6.84e-18 11 239 10 237
RfbF is a putative dTDP-rhamnosyl transferase. Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.
pfam00535 Glycos_transf_2 1.23e-16 6 108 8 113
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
BBL07919.1 1.59e-179 1 330 7 337
BBL10710.1 1.59e-179 1 330 7 337
BBK99894.1 2.25e-179 1 330 7 337
BBL05647.1 6.44e-179 1 330 7 337
CBK63650.1 2.71e-178 1 327 7 334

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6E7I_A 1.65e-06 11 215 109 317
HumanppGalNAcT2 I253A/L310A Mutant with EA2 and UDP [Homo sapiens]
6NQT_A 1.70e-06 11 215 152 360
GalNac-T2soaked with UDP-sugar [Homo sapiens],6NQT_B GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_C GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_D GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_E GalNac-T2 soaked with UDP-sugar [Homo sapiens],6NQT_F GalNac-T2 soaked with UDP-sugar [Homo sapiens]
2FFU_A 2.83e-06 11 215 82 290
CrystalStructure of Human ppGalNAcT-2 complexed with UDP and EA2 [Homo sapiens],2FFV_A Human ppGalNAcT-2 complexed with manganese and UDP [Homo sapiens],2FFV_B Human ppGalNAcT-2 complexed with manganese and UDP [Homo sapiens]
6EGS_A 2.83e-06 11 215 84 292
Crystalstructure of the GalNAc-T2 F104S mutant in complex with UDP-GalNAc [Homo sapiens],6EGS_B Crystal structure of the GalNAc-T2 F104S mutant in complex with UDP-GalNAc [Homo sapiens]
4D0T_A 3.00e-06 11 215 152 360
GalNAc-T2crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_B GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_C GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_D GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_E GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0T_F GalNAc-T2 crystal soaked with UDP-GalNAc, EA2 peptide and manganese [Homo sapiens],4D0Z_A GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_B GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_C GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_D GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_E GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D0Z_F GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 and manganese (Higher resolution dataset) [Homo sapiens],4D11_A GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_B GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_D GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_E GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],4D11_F GalNAc-T2 crystal soaked with UDP-5SGalNAc, mEA2 peptide and manganese (Lower resolution dataset) [Homo sapiens],5AJN_A Crystal structure of the inactive form of GalNAc-T2 in complex with the glycopeptide MUC5AC-Cys13 [Homo sapiens],5AJO_A Crystal structure of the inactive form of GalNAc-T2 in complex with the glycopeptide MUC5AC-3,13 [Homo sapiens],5AJP_A Crystal structure of the active form of GalNAc-T2 in complex with UDP and the glycopeptide MUC5AC-13 [Homo sapiens],5FV9_A Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_B Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_C Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_D Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_E Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5FV9_F Crystal structure of GalNAc-T2 in complex with compound 16d [Homo sapiens],5NDF_A Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_B Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_C Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_D Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_E Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens],5NDF_F Small-molecule inhibition of ppGalNAc-Ts selectively reduces mucin-type O-glycosylation [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P9WMY2 1.83e-20 10 239 17 260
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3 1.83e-20 10 239 17 260
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
P9WMX0 8.87e-16 6 230 92 297
Pre-mycofactocin glycosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=mftF PE=3 SV=1
P9WMX1 8.87e-16 6 230 92 297
Pre-mycofactocin glycosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=mftF PE=1 SV=1
Q50864 5.29e-11 11 214 589 792
O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 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
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001302.1_01418.