CAZyme Information: MGYG000001918_00988

Basic Information

• Species: Prevotellamassilia sp900541575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp900541575
• CAZyme ID: MGYG000001918_00988
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
723		80878.91	7.6539

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001918	2523391	MAG	Denmark	Europe

• Gene Location: Start: 22217; End: 24388 Strand: +

Full Sequence      

MKILLPLLASMLSLSLSAQTVSRMSELNPEQKAAATNIRLTGKLSTTGNSDFRQMRDLCY
QLHSADLSGADCEVIPNNAFHSRHALEKILLPDNLKSIGSQAFFACTRLSQITLPPSLTR
VGDAAFSSCSALKEITINGTPTLGEFAFARLTGLRTVRVNSSVPPVASPSTFDGIDRKRV
KLIVPKGSELKYRKAAGWSIFFSTPDNENKLCNPLEAIVPLPAKIQTLEGASLTTERHWE
VLAAEGLANECTQAERVLRARIPKLKNPKLAGHATLTLGLDPTLSDNEAYVLKVSAKGVD
IHGKTAAGVFYGLMTFDQLLRGDGSSTCCEAIPQLRIEDAPRTHIRELMLDPCRTFIPFD
ELKAFIPEMARYKYNTVHLHLTDDQAWRIEIKKYPELTQKASSRVGMDDMLVPISGYYTQ
SQMRELVAYAAQYHVQVVPEIEMPGHEVAAIHVFPKLTCGEKQVPIRTTCGVSDNLLCPG
SEFTYEFLGNVFRELADIFPSPYIHLGGDEAGHPALDCWTNCDNCKALKKRLGITTTDRS
ENWRLQQYLFDRMIDTLRTKYGKTPMFWYETDFKKIQSGCVTFSWRHGLTKQALEAAVAN
NAKIMLCPGEHCYLDYPMAAGDMPEINWGMPVISLKQSYELDPSWGMDKDFEKNNLFGVA
GTLWSECINSPERIYYQAYPRALALSEVGWSPANKRSWDDFLKRLKPVLNDMQRRGITFS
KQF

Enzyme Prediction     

No EC number prediction in MGYG000001918_00988.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	345	692	2.6e-97	0.9525222551928784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06563	GH20_chitobiase-like	2.09e-144	346	705	4	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	3.83e-115	346	692	4	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	1.29e-98	346	705	4	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.
COG3525	Chb	2.68e-86	151	709	50	632	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	1.73e-68	345	691	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
QUB45992.1	2.03e-260	40	720	48	719
ANR73104.1	2.03e-260	40	720	48	719
QUB40309.1	2.09e-260	51	720	62	740
QUB76505.1	2.33e-259	51	720	57	719
QUB62399.1	2.33e-259	51	720	57	719

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JE8_A	2.83e-89	282	705	32	441	crystalstructure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEA_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835],6JEB_A crystal structure of a beta-N-acetylhexosaminidase [Akkermansia muciniphila ATCC BAA-835]
6Q63_A	6.04e-76	218	721	31	538	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
6EZR_A	2.05e-72	281	721	203	639	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZR_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi [Vibrio harveyi],6EZS_A Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6EZS_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex with N-acetylglucosamine [Vibrio harveyi],6K35_A Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi],6K35_B Crystal structure of GH20 exo beta-N-acetylglucosaminidase from Vibrio harveyi in complex with NAG-thiazoline [Vibrio harveyi]
6EZT_A	2.64e-71	281	721	200	636	Crystalstructure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi],6EZT_B Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase D437A inactive mutant from Vibrio harveyi [Vibrio harveyi]
3RCN_A	3.58e-71	268	705	59	498	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UP57	3.06e-88	282	705	53	462	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
P49008	2.37e-73	218	719	37	532	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155	8.58e-67	217	689	140	604	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UQG6	1.15e-65	219	721	33	531	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
Q7WUL4	9.80e-56	214	705	2	463	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
0.000421	0.998928	0.000172	0.000164	0.000146	0.000147

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001918_00988.