CAZyme Information: MGYG000004133_01568

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514
• CAZyme ID: MGYG000004133_01568
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
454		52448.12	4.7348

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004133	2160156	MAG	United Kingdom	Europe

• Gene Location: Start: 10; End: 1374 Strand: +

Full Sequence      

MEKSEVSDLCDYIRSFGLDVIPEVQSWSHTQYITTAYPELAEVPEGEIKTSKVIDSYAED
IRPAQFYKHSMCPSHERYYDVIFGILDEVLEVVKPQKYVHMGHDEIYELCICEKCKNLNA
GDLYAKEVTTLNNYIKSKNLTMMIWSDMIQERSYKSLSAINKLPKDVIMLDFIWYFHLDQ
DLEDNLLNHGFNVVIGNAYSSYYPRFETRSKKEGIIGAEVSAWVACDEDTYSFEGKMYDY
IYMANCLWNRNYDGAMRLTYDEAMRSILIDTRRRIGELDFNGEEKRLSFKSDRINVPADL
VGYIPYEEAAVVTSDMSEVSIDFNGYAKQFTFVQAMDADADRFAWLPATVIGSYTLNYED
GTSYSRDIRFGDDIHSYRFRFGTPLKSHLFRHEGYIASYSARPECGKTAFGEDYTLFDNF
VKNPTPEKKIVGITLKHNKNTDANIILFDAKATV

Enzyme Prediction     

No EC number prediction in MGYG000004133_01568.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	3	235	5.8e-30	0.6172106824925816

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	8.52e-31	3	223	59	276	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	2.65e-16	3	223	77	317	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06562	GH20_HexA_HexB-like	3.53e-13	3	223	69	297	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.
cd06563	GH20_chitobiase-like	7.59e-13	3	234	85	294	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.
cd06564	GH20_DspB_LnbB-like	8.98e-13	3	203	81	246	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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
QUH29563.1	3.41e-109	1	450	363	829
SDT51451.1	6.66e-42	1	447	215	621
SQF34752.1	7.43e-38	1	447	220	646
ABN44552.1	1.01e-37	1	447	220	646
VDY71689.1	3.52e-37	1	447	220	646

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3U4H6	5.23e-06	4	218	67	261	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000079	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004133_01568.