CAZyme Information: MGYG000001689_01508

Basic Information

• Species: Blautia coccoides
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia coccoides
• CAZyme ID: MGYG000001689_01508
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
628	MGYG000001689_4|CGC4	71977.36	5.3633

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001689	6086770	Isolate	United States	North America

• Gene Location: Start: 266853; End: 268739 Strand: +

Full Sequence      

MGIFNLEHIDPSLIPGAMLTAEYLEKDMGTDRRVDIITEKGASGLSLRLDGNTARITYSR
TTEFFRGLGIIKEWINENRQSAAKEEHPAFEHLTYMADCSRNAVCSPDFLKKLLVKLSLM
GYDRLMLYTEDTYEVEGYPYFGHFRGRYSRQELRELDRFASSLGIEMVPCIQTLAHLNAI
FRWPAFEQVHDTGDILLCKSEDTYRLIEAMIRTWSETFQSRIINIGMDEAEMIGRGTYLN
RFGYEERIDIMERHLHRVLEICEKYGYTAMMWSDMFFKMISGGDYYGKEFHITEEIKKKI
PANVELLYWDYYSRDEETYEQMMKYHRELAPNVGFAGGAWKWNGYAPLLNHSMQVSRLAL
RQCQKHGITNVLVTGWGDDGSEASQSSVLPVLSLFAEYDYTRSVNDCDLAPRLLACTGAV
LQDFLKLDLPNLTPGNLLPGKMSAAPAKYLLYQDVLMGIYDCHVDIQSFPKHYRRCAEEF
RLIAEKGGEYACIFRTLQRLSEVLAAKAVLGIKAKAAYEAEDRAALFETADACINTAGLV
DQFKNALQDQWFRENKSFGYEVLDIRLGGLKERLRSCAARMRDYAEGKIICIEELEEHRL
PLLADKTGQPLSPVCDNIWREMVTASVI

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	86	401	3.7e-37	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	2.14e-100	95	400	4	300	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.
pfam18088	Glyco_H_20C_C	3.23e-65	422	601	1	181	Glycoside Hydrolase 20C C-terminal domain. This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature.
cd02742	GH20_hexosaminidase	5.06e-42	92	397	1	299	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.
cd06564	GH20_DspB_LnbB-like	5.83e-12	148	321	79	234	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.
cd06562	GH20_HexA_HexB-like	3.33e-07	133	276	47	212	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
QMW77717.1	0.0	1	628	8	635
QIB58280.1	0.0	1	628	1	628
QBE99175.1	0.0	1	628	1	628
ANU74916.1	0.0	1	628	1	628
QQQ92469.1	0.0	1	628	1	628

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EPL_X	1.32e-145	34	628	29	624	N-acetyl-B-D-glucosaminidase(GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPM_X N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii [Streptococcus gordonii],2EPN_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPN_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii]
5A69_A	2.01e-141	37	628	54	646	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-PUGNAc [Streptococcus pneumoniae TIGR4],5A6A_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6A_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6J_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_D GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6K_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5A6K_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5AC5_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4],5AC5_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4]
5A6B_A	2.01e-141	37	628	54	646	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5AC4_A	5.65e-141	37	628	54	646	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4],5AC4_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4]
5A6B_D	1.54e-140	37	628	54	645	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3U4H6	1.45e-08	108	376	24	298	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd PE=1 SV=1
Q8WVB3	1.78e-07	108	376	24	298	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
A6QNR0	6.51e-07	109	342	17	242	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2

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 MGYG000001689_01508.