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CAZyme Information: MGYG000000335_01422

You are here: Home > Sequence: MGYG000000335_01422

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 Enterococcus_G italicus
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_G; Enterococcus_G italicus
CAZyme ID MGYG000000335_01422
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
354 40606.4 6.2444
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000335 1887038 MAG Sweden Europe
Gene Location Start: 691;  End: 1755  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000335_01422.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 1 347 1.7e-120 0.9942857142857143

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3589 COG3589 1.03e-111 1 351 3 360
Uncharacterized protein [Function unknown].
pfam19200 DUF871_N 1.70e-101 3 230 2 233
DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
pfam05913 DUF871 1.06e-36 242 348 7 116
Bacterial protein of unknown function (DUF871). This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
cd06565 GH20_GcnA-like 0.005 64 135 5 72
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
QEA60502.1 2.29e-117 1 351 1 350
AIS03849.1 2.29e-117 1 351 1 350
ALS00837.1 2.37e-117 1 350 1 351
QRZ11657.1 1.86e-116 1 351 1 350
QIT58302.1 1.06e-115 1 351 1 351

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2P0O_A 4.74e-102 2 350 5 360
Crystalstructure of a conserved protein from locus EF_2437 in Enterococcus faecalis with an unknown function [Enterococcus faecalis V583]
1X7F_A 1.57e-33 3 349 30 385
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2XHV5 2.86e-51 1 346 1 342
6-phospho-N-acetylmuramidase OS=Staphylococcus aureus (strain USA300) OX=367830 GN=mupG 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
1.000075 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000335_01422.