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CAZyme Information: MGYG000000193_00672

You are here: Home > Sequence: MGYG000000193_00672

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 KLE1615 sp900066985
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; KLE1615; KLE1615 sp900066985
CAZyme ID MGYG000000193_00672
CAZy Family GH28
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
970 MGYG000000193_5|CGC2 108267.65 5.025
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000193 4116467 Isolate China Asia
Gene Location Start: 64894;  End: 67806  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000193_00672.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH28 51 369 1e-36 0.7476923076923077

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG5434 Pgu1 3.42e-38 5 392 65 429
Polygalacturonase [Carbohydrate transport and metabolism].
pfam00583 Acetyltransf_1 1.65e-07 824 944 10 116
Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
COG0456 RimI 5.29e-05 819 948 27 153
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis].
cd04301 NAT_SF 8.13e-04 849 930 1 65
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate. NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
pfam13508 Acetyltransf_7 0.001 845 944 1 81
Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ93914.1 1.09e-312 1 842 1 865
CBL02329.1 9.06e-276 4 760 45 801
AXB28928.1 1.66e-275 4 760 63 819
AHG93184.1 2.85e-96 39 655 50 492
QOY86475.1 3.89e-94 27 655 28 477

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3JUR_A 1.19e-10 27 278 32 287
Thecrystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_B The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_C The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima],3JUR_D The crystal structure of a hyperthermoactive Exopolygalacturonase from Thermotoga maritima [Thermotoga maritima]
4MXN_A 2.33e-08 39 250 37 215
Crystalstructure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_B Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_C Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184],4MXN_D Crystal structure of a putative glycosyl hydrolase (PARMER_00599) from Parabacteroides merdae ATCC 43184 at 1.95 A resolution [Parabacteroides merdae ATCC 43184]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000050 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000193_00672.