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CAZyme Information: MGYG000001787_00728

You are here: Home > Sequence: MGYG000001787_00728

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 Phocaeicola sp900551645
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900551645
CAZyme ID MGYG000001787_00728
CAZy Family GT2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
339 39088.96 6.8852
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001787 3320861 MAG Denmark Europe
Gene Location Start: 38855;  End: 39874  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001787_00728.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 4 115 3.8e-22 0.6823529411764706

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1216 GT2 1.47e-51 1 290 3 295
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism].
cd04186 GT_2_like_c 1.51e-51 5 222 1 166
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.
pfam00535 Glycos_transf_2 2.42e-20 4 152 1 149
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.
TIGR03965 mycofact_glyco 8.23e-19 3 220 76 280
mycofactocin system glycosyltransferase. Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.
cd00761 Glyco_tranf_GTA_type 7.70e-18 5 130 1 128
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRO24852.1 1.01e-180 2 337 3 338
ADY35585.1 1.79e-175 1 339 5 343
QQT78972.1 1.34e-172 1 337 1 337
ASM67710.1 1.34e-172 1 337 1 337
QRP59721.1 1.34e-172 1 337 1 337

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6E7I_A 1.36e-07 15 261 109 375
HumanppGalNAcT2 I253A/L310A Mutant with EA2 and UDP [Homo sapiens]
6NQT_A 1.40e-07 15 261 152 418
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 4.10e-07 15 261 82 348
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 4.11e-07 15 261 84 350
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 4.37e-07 15 261 152 418
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 1.57e-17 3 220 5 235
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=wbbL PE=3 SV=2
P9WMY3 1.57e-17 3 220 5 235
N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=wbbL PE=1 SV=2
P55465 2.03e-15 3 256 627 881
Uncharacterized protein y4gI OS=Sinorhizobium fredii (strain NBRC 101917 / NGR234) OX=394 GN=NGR_a03550 PE=4 SV=1
Q50864 4.16e-14 2 229 575 801
O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 SV=1
P46370 7.45e-09 3 235 132 344
Uncharacterized 55.3 kDa protein in thcA 5'region OS=Rhodococcus erythropolis OX=1833 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
1.000068 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001787_00728.