CAZyme Information: MGYG000004754_03607

Basic Information

• Species: Elizabethkingia bruuniana
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Elizabethkingia; Elizabethkingia bruuniana
• CAZyme ID: MGYG000004754_03607
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
773	MGYG000004754_8|CGC1	89449.17	9.3344

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004754	4072783	MAG	China	Asia

• Gene Location: Start: 25427; End: 27748 Strand: +

Full Sequence      

MRITKIFKVLLFLFSVSLFSQNKISEETGEIPKVKKGDLRITNPVAPKGYKLKLMGSDAF
PVIDIKGNIIQPLVPTEVNLYYVLSNEKDTLQQFDINRQVVIPGRYNDNGKNHKPFVIPS
LREWYGRNGDFKLSSTAKIIVDTRDKEKLKNLASLLQKEIKDFSGLEPKIAYGKNEGTGN
IYLSLQHQDQSLGEEGYYCNIENNFEIFALQYQGLFWGTRTFLQLLEQQPKERIFPKGEI
RDYPKYKVRGFVLDAGRKFFSLDFLNKYVKLMSYYKMNDFHIHLNDNGFKIYFDNNWDKT
YSGFRLENATYPELATKNEFYTKNEFREFQKMAQNYAVRIIPEIDVPAHSLAITKAVPDI
GSNKYGRDHLDINLPKTYEVVENIFKEYLEGTDPVFVGKEVHIGTDEYDKTEAEAFRKFT
DHFMDYVQSFGKDVRLWGALTHAKGKTPVRSKNIIMNTWYNGYADPIEMKKLGYKQISTP
DGILYIVPKAGYYYDYLNIENIYKKWEPRMIGNITFPLGDPTIIGGSFAVWNDIAGNGIT
DKDVHDRVFPAMQVLAEKMWRGTVSAPDFNYFSQNAGLISEGPFLNIRGKYDKKGISFPL
MVKQQDVRIHRAEWVKAGKEEYLDFKGADSYAEFSLPEIGYNYTVSFDIKPVVENNQKMP
VFTSSDAMLYLKNGKLRFSRDGYDDSFDYKFPRGSWTKATITGNNEGVKLFINGVLQQDL
TNEWRTYNDKDKTKRRKMYTLFFPLQKIGGFEGSLKNIVINNKLLSDQEIKMK

Enzyme Prediction     

No EC number prediction in MGYG000004754_03607.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	242	561	5.6e-73	0.9673590504451038

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	6.53e-127	247	562	1	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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	1.75e-49	246	560	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	2.13e-44	249	561	2	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	9.71e-41	249	560	4	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.
cd06562	GH20_HexA_HexB-like	3.64e-39	246	560	1	322	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
ATL42130.1	0.0	1	773	1	773
AQX85364.1	0.0	1	773	1	773
QQN59020.1	0.0	1	773	1	773
QDZ62174.1	0.0	96	773	1	678
QNR84812.1	2.88e-310	18	770	18	775

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.03e-91	31	755	9	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	5.80e-31	114	589	38	516	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]
6YHH_A	3.79e-28	194	560	91	476	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
4H04_A	5.68e-27	114	614	33	525	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
4PYS_A	7.34e-22	180	560	64	462	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
B2UPR7	1.73e-95	31	755	31	748	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
Q54SC9	4.95e-21	176	583	85	507	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 SV=1
Q9SYK0	7.52e-20	214	562	138	524	Beta-hexosaminidase 2 OS=Arabidopsis thaliana OX=3702 GN=HEXO2 PE=1 SV=1
P49008	8.24e-19	98	415	24	343	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7WUL4	2.02e-18	164	584	52	469	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
0.001340	0.789609	0.208317	0.000245	0.000251	0.000228

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004754_03607.