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CAZyme Information: MGYG000000084_02079

You are here: Home > Sequence: MGYG000000084_02079

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 Gemmiger formicilis
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger; Gemmiger formicilis
CAZyme ID MGYG000000084_02079
CAZy Family GT6
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
280 MGYG000000084_9|CGC1 33926.19 8.6828
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000084 3006488 Isolate United Kingdom Europe
Gene Location Start: 47625;  End: 48467  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000084_02079.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT6 3 215 1.6e-59 0.7535714285714286

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02515 Glyco_transf_6 8.70e-28 4 229 36 256
Glycosyltransferase family 6 comprises enzymes responsible for the production of the human ABO blood group antigens. Glycosyltransferase family 6, GT_6, comprises enzymes with three known activities: alpha-1,3-galactosyltransferase, alpha-1,3 N-acetylgalactosaminyltransferase, and alpha-galactosyltransferase. UDP-galactose:beta-galactosyl alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the transfer of galactose from UDP-alpha-d-galactose into an alpha-1,3 linkage with beta-galactosyl groups in glycoconjugates. The enzyme exists in most mammalian species but is absent from humans, apes, and old world monkeys as a result of the mutational inactivation of the gene. The alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase are responsible for the production of the human ABO blood group antigens. A N-acetylgalactosaminyltransferases use a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase uses a UDP-galactose donor to convert the H-antigen acceptor to the B antigen. Alpha-1,3 N-acetylgalactosaminyltransferase and alpha-galactosyltransferase differ only in the identity of four critical amino acid residues.
pfam03414 Glyco_transf_6 6.86e-25 10 229 59 273
Glycosyltransferase family 6.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBG40459.1 1.58e-65 3 241 44 279
SQH71958.1 1.58e-65 3 241 44 279
QXD33209.1 1.80e-63 2 256 3 256
AZM39251.1 2.03e-63 2 212 7 216
ARS38480.1 3.60e-63 1 234 1 228

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4AYJ_A 4.59e-57 3 233 2 233
Molecularstructure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen [Bacteroides ovatus],4AYJ_B Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen [Bacteroides ovatus],4AYJ_C Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen [Bacteroides ovatus],4AYJ_D Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen [Bacteroides ovatus],4AYL_A Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen [Bacteroides ovatus]
4CJB_A 1.29e-56 3 233 2 233
orthorhombiccrystal form of Bogt6a E192Q in complex with GalNAc [Bacteroides ovatus],4CJB_B orthorhombic crystal form of Bogt6a E192Q in complex with GalNAc [Bacteroides ovatus],4CJB_C orthorhombic crystal form of Bogt6a E192Q in complex with GalNAc [Bacteroides ovatus],4CJB_D orthorhombic crystal form of Bogt6a E192Q in complex with GalNAc [Bacteroides ovatus],4CJC_A orthorhombic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP, GalNAc [Bacteroides ovatus],4CJC_B orthorhombic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP, GalNAc [Bacteroides ovatus],4CJC_C orthorhombic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP, GalNAc [Bacteroides ovatus],4CJC_D orthorhombic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP, GalNAc [Bacteroides ovatus]
4CJ8_A 1.37e-56 3 233 4 235
monocliniccrystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_B monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_C monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_D monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_E monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_F monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_G monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_H monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_I monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_J monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_K monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_L monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_M monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_N monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_O monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus],4CJ8_P monoclinic crystal form of Bogt6a E192Q in complex with UDP-GalNAc, UDP and GalNAc [Bacteroides ovatus]
3SX7_A 1.14e-23 4 221 55 274
Crystalstructure of ABBA+UDP+Gal with Glycerol as the cryoprotectant [Homo sapiens],3SX8_A Crystal structure of ABBA+UDP+Gal with MPD as the cryoprotectant [Homo sapiens]
4FRA_A 1.16e-23 4 221 55 274
CrystalStructure of ABBA+UDP+Gal at pH 5.0 with MPD as the cryoprotectant [Homo sapiens],4FRB_A Crystal Structure of ABBA+UDP+Gal at pH 8.0 with MPD as the cryoprotectant [Homo sapiens],4FRD_A Crystal Structure of ABBA+UDP+Gal at pH 9.0 with MPD as the cryoprotectant [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P16442 2.10e-22 4 221 116 335
Histo-blood group ABO system transferase OS=Homo sapiens OX=9606 GN=ABO PE=1 SV=2
Q5ZLK4 6.28e-21 4 223 107 321
Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 OS=Gallus gallus OX=9031 GN=GBGT1 PE=2 SV=1
Q8N5D6 3.01e-19 4 223 111 325
Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 OS=Homo sapiens OX=9606 GN=GBGT1 PE=1 SV=2
Q9ET32 4.18e-19 4 221 111 330
Histo-blood group ABO system transferase 1 OS=Rattus norvegicus OX=10116 GN=Abo PE=1 SV=1
Q8CFC4 6.79e-19 4 221 97 316
Histo-blood group ABO system transferase 2 OS=Rattus norvegicus OX=10116 GN=Abo2 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
1.000063 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000084_02079.