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CAZyme Information: MGYG000004709_00463

You are here: Home > Sequence: MGYG000004709_00463

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 QAMX01 sp003149835
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; QAMX01; QAMX01; QAMX01 sp003149835
CAZyme ID MGYG000004709_00463
CAZy Family GH163
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
573 65218.37 4.9432
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004709 2240013 MAG China Asia
Gene Location Start: 4065;  End: 5786  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004709_00463.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH163 196 452 1e-92 0.9840637450199203

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam16126 DUF4838 3.97e-112 185 452 1 263
Domain of unknown function (DUF4838). This family consists of several uncharacterized proteins found in various Bacteroides and Chloroflexus species. The function of this family is unknown.
cd06565 GH20_GcnA-like 0.002 203 380 92 230
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASV73444.1 1.21e-112 8 568 24 597
AIF26900.1 3.96e-102 19 500 13 528
QQL44163.1 1.10e-97 68 532 81 541
QNN24856.1 9.94e-97 76 471 104 503
AIE83908.1 1.23e-94 19 513 20 511

PDB Hits      help

has no PDB hit.

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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004709_00463.