logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001659_01864

You are here: Home > Sequence: MGYG000001659_01864

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 Paraprevotella sp900760455
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900760455
CAZyme ID MGYG000001659_01864
CAZy Family GT2
CAZyme Description 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
425 48382.68 7.9829
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001659 3410285 MAG United States North America
Gene Location Start: 31733;  End: 33010  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001659_01864.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 10 125 3.6e-20 0.6941176470588235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06433 GT_2_WfgS_like 3.28e-63 10 210 1 201
WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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.
cd04647 LbH_MAT_like 3.25e-38 303 407 1 109
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
PRK10502 PRK10502 2.36e-32 260 410 25 178
putative acyl transferase; Provisional
cd05825 LbH_wcaF_like 4.18e-31 301 407 1 107
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.
cd03357 LbH_MAT_GAT 2.31e-29 275 407 34 169
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AXV50072.1 1.73e-154 8 425 4 421
QUI93290.1 7.00e-154 8 425 4 421
QUB91771.1 1.41e-153 8 425 4 421
QJR60740.1 1.47e-68 6 236 2 233
QJR54460.1 1.47e-68 6 236 2 233

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ECT_A 9.05e-16 275 413 48 191
CrystalStructure of the Hexapeptide-Repeat Containing-Acetyltransferase VCA0836 from Vibrio cholerae [Vibrio cholerae],3NZ2_A Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_B Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_C Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_D Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_E Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_F Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_G Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_H Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_I Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_J Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_K Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_L Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961]
1KQA_A 1.24e-12 275 417 47 191
GalactosideAcetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_B Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_C Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KRR_A Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_B Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_C Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRU_A Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_B Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_C Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRV_A Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_B Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_C Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli]
3CJ8_A 2.10e-09 356 409 165 218
Crystalstructure of 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase from Enterococcus faecalis V583 [Enterococcus faecalis],3CJ8_B Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase from Enterococcus faecalis V583 [Enterococcus faecalis],3CJ8_C Crystal structure of 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase from Enterococcus faecalis V583 [Enterococcus faecalis]
3FTT_A 4.26e-09 306 421 77 195
ChainA, Putative acetyltransferase SACOL2570 [Staphylococcus aureus subsp. aureus COL]
5U2K_A 7.79e-09 306 421 77 195
ChainA, Galactoside O-acetyltransferase [Staphylococcus aureus subsp. aureus COL]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P71239 3.15e-18 10 208 4 201
Putative colanic acid biosynthesis glycosyl transferase WcaE OS=Escherichia coli (strain K12) OX=83333 GN=wcaE PE=4 SV=2
P9WMX9 7.53e-16 7 109 5 108
Uncharacterized glycosyltransferase Rv1514c OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1514c PE=1 SV=1
P9WMX8 7.53e-16 7 109 5 108
Uncharacterized glycosyltransferase MT1564 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1564 PE=3 SV=1
P37515 7.58e-13 275 409 46 183
Probable maltose O-acetyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=maa PE=3 SV=1
P07464 6.81e-12 275 417 47 191
Galactoside O-acetyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=lacA 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
1.000055 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
231 253