CAZyme Information: MGYG000003856_01888

Basic Information

• Species: Paramuribaculum sp900551515
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900551515
• CAZyme ID: MGYG000003856_01888
• CAZy Family: GH20
• CAZyme Description: Beta-hexosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
519	MGYG000003856_134|CGC1	59232.5	6.1477

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003856	2220083	MAG	United States	North America

• Gene Location: Start: 128; End: 1687 Strand: +

Full Sequence      

MKLKITPIFIILSAALDLAAQSVIPSPRRFAAREGSFCIGREIAICCNDTTAGYFTLFRD
EFAAGAGLHLTCDTINSDVAWITDSTIPTEGYEIDITPRRMEIRASDAGGFVYAVQTLRQ
LAVSTSRGIEFRCMSVSDEPRMRWRAFMLDSGRQFQPVEVIKKYIDMASMLKMNRFHWHL
TEGLGWRIEIKRYPLLALKGAFVGKSPGQQGYYTQDEIRMLVDYARRRKIEIVPEIDMPG
HAEAAIFSYPGLGCFGDRIEIPQTGFTPNIFCAGNDSTLVFLKNVLDEVCELFPSEYIHL
GGDEAPKDNWEKCPSCRARLEREHLADTHALQLWLSAEMARHLKSKGRKAIFWDDVVAGE
GYRLPDNSVIQWWNYRGHGSRGLRNALSCGLEVICSPNYYTYLNFPLTPWRGYGQKRTFD
LADVYLRNPADSAFNEGNPSVMGMTCALWTDYGVTEDMIDRRLFPRILALAEQMWHRDDT
TPHPEDFYRRIDAARPFWESEGYEFGPAFRQDVPPGYTW

Enzyme Prediction     

No EC number prediction in MGYG000003856_01888.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	141	477	4.1e-102	0.9614243323442137

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	8.93e-154	144	491	3	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.
pfam00728	Glyco_hydro_20	4.26e-125	144	476	3	344	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	3.51e-84	23	517	136	655	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	1.82e-80	144	476	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.
cd06570	GH20_chitobiase-like_1	3.84e-80	144	491	3	311	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT71939.1	6.39e-237	1	519	1	518
QMW88593.1	6.39e-237	1	519	1	518
AAO76728.1	6.39e-237	1	519	1	518
ALJ41007.1	6.39e-237	1	519	1	518
QUT39423.1	1.05e-235	1	519	1	518

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PYS_A	3.30e-218	13	519	1	505	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]
7DUP_A	2.13e-83	22	506	5	521	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6Q63_A	7.71e-83	90	505	106	536	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
7DVB_A	1.16e-82	22	506	5	521	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]
7CBN_A	1.95e-81	57	505	50	510	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UQG6	1.00e-80	13	505	24	529	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
P49008	1.24e-80	22	494	36	521	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	2.96e-65	15	471	133	601	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	4.90e-64	86	519	54	489	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	6.69e-49	90	519	82	485	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
0.000372	0.998973	0.000181	0.000159	0.000150	0.000147

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003856_01888.