CAZyme Information: MGYG000001489_03642

Basic Information

• Species: Parabacteroides goldsteinii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii
• CAZyme ID: MGYG000001489_03642
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
369	MGYG000001489_2|CGC17	42268.35	5.9651

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001489	6453137	Isolate	not provided	not provided

• Gene Location: Start: 1168867; End: 1169976 Strand: -

Full Sequence      

MKHFITIACLLICITTNGIFAQTNVNMLDSILPVRGLAIAAPSVQKMDVFLKFIEEELAP
GHFNLLILRVDWNYAYESHPELRDPNPLTLQDVKRIVATCRKHNIRIAPQINLLGHQSWA
ETTYALLREYPEFDETPHVDTKNYTGWPNPDGLYCKSYCPLHPDVHKVVFALVDELTDAF
ETDLFHAGMDEVFYIGDDKCPRCSGRDKAELYAGEVTKIQNHLAQQGKRLMIWGDRLIDG
KTTGIGAWEASMNNTYRAIDLIPKEVFICDWHYERPEQTAVYFAMKGFDVATCPWRKPEV
ALKQLDDMKRFRQQSGSQMSNRFQGIIETVWSGADGFLENYYKPESEQQEVSDVVTIKKL
ISAYKSMSK

Enzyme Prediction     

No EC number prediction in MGYG000001489_03642.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	71	304	1.4e-31	0.6201780415430267

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	2.15e-28	44	339	13	284	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.
pfam00728	Glyco_hydro_20	1.14e-16	89	294	76	261	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	5.70e-13	89	248	84	241	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. 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.
cd02742	GH20_hexosaminidase	2.22e-11	35	239	2	196	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
cd06562	GH20_HexA_HexB-like	8.08e-10	89	259	68	245	Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUR50380.1	1.89e-226	1	367	1	367
BBK91426.1	1.89e-226	1	367	1	367
QRO16628.1	2.68e-226	1	367	1	367
QCY56661.1	2.68e-226	1	367	1	367
QUT19316.1	2.68e-226	1	367	1	367

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	1.20e-09	89	233	166	307	crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UP57	6.85e-09	89	233	187	328	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000226	0.999158	0.000152	0.000151	0.000140	0.000129

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001489_03642.