CAZyme Information: MGYG000003445_00084

Basic Information

• Species: RC9 sp900767375
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900767375
• CAZyme ID: MGYG000003445_00084
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
440		49940.74	4.8891

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003445	1789928	MAG	Fiji	Oceania

• Gene Location: Start: 773; End: 2095 Strand: -

Full Sequence      

MRTILFIILSLFPVPVREVYSEGEYTCRKVESGVSFLLDETVPAEGYEIDVTESSATVRY
SDKGGLFYARQAIGQISVTKADGSVSIPCCSITDYPRVAWRGFMLDSGRQYQSPETIMRL
LDMMAALKMNVFHWHLTDGLGWRIDVKRYPRLTETGSCVAEGPQQQGYYTRKEIREIVSY
AAVRNITVVPEIDMPGHAEAALTAYPELSCFGIPAEIPKAGYTQVIFCAGKDRTLRFLED
VLDEVCRLFPSEYIHLGGDEAPKGNWDKCPDCIRRISEEGLRDSHELQSWFSARMAGYLK
KKGRKAIFWEDVLHPGSTLSPNPLPDNVAIQWWNYRGYGDFALREALANGYELICSPNYF
TYLNFPTEPWKGYEENRTFSFEDAWLHNPVEKGLSSGNPLVLGGECALWTDYGLTEDMLD
ERLFPRIYAIAQLFWSGVSR

Enzyme Prediction     

No EC number prediction in MGYG000003445_00084.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	99	437	4.9e-106	0.9554896142433235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	9.06e-159	99	437	2	344	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.
pfam00728	Glyco_hydro_20	2.41e-132	99	437	2	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06570	GH20_chitobiase-like_1	2.78e-96	99	436	2	297	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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.
COG3525	Chb	2.91e-94	44	436	205	614	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	1.22e-88	100	436	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCA51031.1	2.75e-193	18	435	30	444
QUT71939.1	4.02e-193	18	435	61	475
QMW88593.1	5.70e-193	18	435	61	475
QQA10049.1	5.70e-193	18	435	61	475
AAO76728.1	5.70e-193	18	435	61	475

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PYS_A	3.20e-178	21	437	54	464	Thecrystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343],4PYS_B The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343]
7CBN_A	1.07e-85	29	436	62	482	Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
7DUP_A	5.33e-81	26	436	60	492	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A	2.93e-80	26	436	60	492	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6Q63_A	3.44e-77	45	436	106	508	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	5.24e-86	45	440	111	508	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	7.77e-85	29	436	81	501	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
P96155	3.80e-65	41	431	204	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.24e-64	10	439	26	451	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
Q7WUL4	2.29e-50	9	437	51	450	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 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
0.000343	0.998963	0.000190	0.000168	0.000154	0.000150

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003445_00084.