CAZyme Information: MGYG000004080_00469

Basic Information

• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Arcanobacterium_A
• CAZyme ID: MGYG000004080_00469
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
963		102719.15	5.4942

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004080	1753974	MAG	United Kingdom	Europe

• Gene Location: Start: 208463; End: 211354 Strand: -

Full Sequence      

MGIISAYKRMLAATLTSVLTLLSLSALTAIPAAAEESENLALKATVTACGQEVAGKFAPA
HAADGVWAPADRAANGHAVPPAIHNAADASRWSANSGNGPWWIQYEFPAEVRIDSVTAEW
GNTFATSYYLEVSEDGVSWQKIADGLKATKQTEKVTTTLHNPVTAHYLRLTATKKSQNFS
LSLWELAVHGEMIGRPLTNDATSITPKPLSADISKNADPFVFTSDTCISLSSKDLEPALD
ILRETLEKSYDLALPARGDCAIHIDLDPHFKAPRGQANESYQLVVTDKNITITASRVRGA
IWAVQSLIQLIGPWASAQAQVAEPAAVPQVRVIDAPRYAWRGVMLDPCRSFIPVDEIKKY
VDLMSTSKLNVLHMHISEDQGWRLEISNDGKEAGDSIDYEQLIKKSSLTSYMAGSSHMAP
EAGRTGYYTKADYADIIRYAASRGIAVITEVDGPGHTNSALHAIPELNTAGASPKPPAGA
TTTAPFVDGKDGFGTLDLKSEATYTFMRHVIADIAKQHSDALASISNSALRAEVTLPYFH
IGGDESTGAGEGYKNYIGRLSDIARQESFTPIVWNDALAKAPDSLAEGSVVQHWTGSTAA
LSAFTKNKNGKVLMSTVNNAYYPQRPGSDVAGPTWACAQGCTLSNWYNWDPTAQAGVAES
SVLGVESALWQEHLRTDHDAQFVMFPRTFALAEVAWSQNSAKDYDDFRSRLAARGIDLIN
RGVTFRLSAPNDVDAVAWAGAYSFLAQEKNSALSSTQAADIGLLALPGVTAADTSRLPLT
ASLIDKQGVEHQMHISYAMERAFNYSDEGKTTGRQMNSIIRVKATLAQPICAGGAGTPAN
AVTEGTLRISGTIPADNRAPELALNAADMAVKVSEECPPGVSDSGTGPNQPGQPDLGESG
EPSEPNPTPEADLHNATASSVKNGNSASIRHMPSTGSQTGLAALISFVLLVAGVLLVKHR
QHE

Enzyme Prediction     

No EC number prediction in MGYG000004080_00469.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	333	698	1e-82	0.973293768545994
CBM32	81	187	4e-18	0.8548387096774194

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06568	GH20_SpHex_like	5.97e-97	338	711	1	329	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
pfam00728	Glyco_hydro_20	1.48e-82	338	698	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.46e-78	338	711	1	357	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	5.05e-60	340	697	1	303	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	6.66e-59	338	715	1	348	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
QGH70671.1	7.55e-216	22	867	26	847
BBA55227.1	1.07e-201	39	832	3	797
BBA49032.1	1.07e-201	39	832	3	797
BAQ98211.1	1.07e-201	39	832	3	797
ALE11422.1	1.43e-201	32	832	38	843

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YXZ_JJJ	1.24e-203	32	832	9	814	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
6Z14_JJJ	3.48e-203	32	832	9	814	ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]
3GH4_A	8.39e-63	278	725	121	519	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
4C7D_A	1.05e-62	208	714	11	474	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
4C7G_A	2.72e-62	208	714	11	474	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7WUL4	1.83e-52	203	712	5	464	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
P49008	1.56e-48	181	730	14	537	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	1.63e-47	279	726	97	530	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
B2UP57	7.75e-36	279	712	58	463	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
P96155	3.44e-33	196	692	132	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI 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
0.000384	0.998702	0.000221	0.000315	0.000183	0.000157

TMHMM  Annotations     

start	end
935	957