CAZyme Information: MGYG000001489_01670

Basic Information

• Species: Parabacteroides goldsteinii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides goldsteinii
• CAZyme ID: MGYG000001489_01670
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
669	MGYG000001489_1|CGC44	77709.4	6.9453

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001489	6453137	Isolate	not provided	not provided

• Gene Location: Start: 2200616; End: 2202625 Strand: +

Full Sequence      

MKQKLFITFILCVWIPVAYATGIPNLLPWPQQVDWNKQTFSGKEIALQTEGNTEQMVTAW
LQENNIGINPASKHKLQIKLVKELPEAKLNANEAYKLQVSSQGITIEATTEQGIYWAIQT
LRQLTEKKGDRAYITGCRITDWPAFRIRGFMQDVGRSYISLEELKREIAILSRYKINVFH
WHLTENQSWRLESKVFPMINDSINTTRMPGKYYTLEEAKELVAFCKQHQVMLIPELDMPG
HSAAFERTFRHDMQSPEGMKILKLLIEEVCETFDMPYLHIGTDEVEFTNPRFVPEMVAFV
RSKGKKAISWNPGWHYQPGEIDMTHLWSYRGKAQPGIPAIDSRFHYLNHFDTFADIRALY
NSTVYRHTEGSDDMAGVILAVWNDRLVQPEENMIRENHLYPNMLAIADRAWRGGGYEYFD
KEGTNLPSEDSRAYTSFAEFEQRMLWHKEHHFKGYPFSYVKQTNVKWRITDAFSNNGDLN
SVFPPETALQNSYTYDGKTYETNETIGAGIYLRHVWGTLVPGFYKDPKENHTAYAWTWVY
SPKDQEAGAWIEFQNYGRSEMDLAPPQGKWDYKGSRIWLNDRELLPPEWTATHTVKSNEI
ALGNENCVAREPLRVHLQKGWNKVFLKLPVGKFTLPEVRLNKWMFTFVFVTPDGEKAVDG
LVYSPDKKK

Enzyme Prediction     

No EC number prediction in MGYG000001489_01670.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	141	412	1.1e-58	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	6.84e-90	147	412	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.
cd06563	GH20_chitobiase-like	2.37e-45	145	411	1	342	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	1.26e-41	145	411	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525	Chb	1.84e-37	26	500	136	702	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06568	GH20_SpHex_like	1.07e-35	145	411	1	314	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT50180.1	0.0	1	669	1	669
ADV44725.1	0.0	3	667	1	668
QQY43256.1	0.0	1	669	1	668
QEW35773.1	0.0	17	669	17	668
BAC56896.1	0.0	2	669	4	670

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EZR_A	6.09e-36	18	285	134	439	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]
6YHH_A	1.26e-35	25	411	8	476	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
6EZT_A	6.31e-35	18	285	131	436	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]
7DUP_A	3.29e-34	93	284	79	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
4PYS_A	5.83e-34	93	467	78	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P96155	1.26e-31	15	285	131	436	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P49008	8.10e-30	93	284	111	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q619W7	3.89e-28	91	411	111	499	Beta-hexosaminidase A OS=Caenorhabditis briggsae OX=6238 GN=hex-1 PE=3 SV=2
Q7WUL4	1.03e-27	76	411	69	448	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
Q22492	2.33e-24	91	411	114	502	Beta-hexosaminidase A OS=Caenorhabditis elegans OX=6239 GN=hex-1 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
0.000239	0.999091	0.000178	0.000159	0.000153	0.000143

TMHMM  Annotations     

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