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CAZyme Information: MGYG000004232_01485

You are here: Home > Sequence: MGYG000004232_01485

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 Terrisporobacter sp900557165
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Terrisporobacter; Terrisporobacter sp900557165
CAZyme ID MGYG000004232_01485
CAZy Family GT6
CAZyme Description O-antigen biosynthesis glycosyltransferase WbnI
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
259 30669.98 5.4522
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004232 2591540 MAG United Kingdom Europe
Gene Location Start: 9237;  End: 10016  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004232_01485.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT6 6 223 4.4e-69 0.7928571428571428

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam03414 Glyco_transf_6 1.42e-37 15 218 61 269
Glycosyltransferase family 6.
cd02515 Glyco_transf_6 3.42e-37 14 216 43 246
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ARS38480.1 2.45e-96 4 258 1 254
QXD33209.1 1.32e-93 5 241 3 244
QKJ30432.1 1.32e-92 7 240 2 237
QEL00979.1 1.39e-79 4 242 1 239
ARS40442.1 1.99e-79 6 238 2 234

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4AYJ_A 1.76e-75 6 238 2 243
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 5.02e-75 6 238 2 243
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 5.35e-75 6 238 4 245
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]
3I0H_A 2.09e-29 6 215 47 264
ChainA, ABO glycosyltransferase [Homo sapiens],3I0I_X Chain X, ABO glycosyltransferase [Homo sapiens],3I0J_A Chain A, ABO glycosyltransferase [Homo sapiens],3I0K_A Chain A, ABO glycosyltransferase [Homo sapiens],3I0L_A Chain A, ABO glycosyltransferase [Homo sapiens]
3I0C_A 2.09e-29 6 215 47 264
ChainA, ABO glycosyltransferase [Homo sapiens],3I0D_A Chain A, ABO glycosyltransferase [Homo sapiens],3I0E_A Chain A, ABO glycosyltransferase [Homo sapiens],3I0F_A Chain A, ABO glycosyltransferase [Homo sapiens],3I0G_A Chain A, ABO glycosyltransferase [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5JBG6 1.09e-39 7 234 3 231
O-antigen biosynthesis glycosyltransferase WbnI OS=Escherichia coli OX=562 GN=wbnI PE=1 SV=1
P38649 7.30e-27 6 238 94 331
Histo-blood group ABO system transferase OS=Mus musculus OX=10090 GN=Abo PE=1 SV=2
P16442 1.43e-26 6 215 115 332
Histo-blood group ABO system transferase OS=Homo sapiens OX=9606 GN=ABO PE=1 SV=2
Q9ET32 6.56e-24 3 238 105 347
Histo-blood group ABO system transferase 1 OS=Rattus norvegicus OX=10116 GN=Abo PE=1 SV=1
Q8CFC4 1.04e-23 3 238 91 333
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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004232_01485.