CAZyme Information: MGYG000003934_00409

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; Borkfalkia
• CAZyme ID: MGYG000003934_00409
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504	MGYG000003934_4|CGC1	58645.79	5.292

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003934	2233390	MAG	United Kingdom	Europe

• Gene Location: Start: 89731; End: 91245 Strand: +

Full Sequence      

MNDISCIKLFLPARDKINYFLEVLRFCSDFGINTLMLEIGGAMEYKRHPEINVGWVEYAS
HFRGSPDAAFRAQYANNFPKNAIHWENGGGSFLKQDEIKRIVAFCAQMGISVIPELPTLT
HCDYFLYSHHDLAERKEDRFADHYCPSNEKVYTLLFDLLDEIIDVFQPSVINIGHDELYT
VCLCERCRKREAAELYAEDIDRIYTYLSGKNIRTAMWADKLYPSKTKKGTAFGGSELKME
YRPEEGGGTVTVPAVWRAAELLPKDILLFHWHYLFGEAAEDYFETLGFEYVFANLNPLTM
PDMRKRFAKTRCRGFCLSNWSGIDKVLLQRNGIFFDVAFMRAYQDGICSDVQPLDEILEI
VSKIVCDYRTAKIKDYIIVEHASLTAVPHRDFCDGNYMDYQKDCLGEYRIYYEDGSIQTE
KIYFGLNINQKYMNYTRQSDEDFYLYDVDRYLVESVYTCVYKIAGGETKYRRFFPRASDS
LIRKWEFCPAVYGNVVETYKLSEG

Enzyme Prediction     

No EC number prediction in MGYG000003934_00409.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	68	278	8.5e-31	0.5459940652818991

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	1.20e-27	16	273	15	212	Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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	7.22e-15	85	219	67	221	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	3.27e-14	61	230	34	204	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	2.95e-13	61	177	36	157	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.
cd06564	GH20_DspB_LnbB-like	4.50e-12	28	228	27	211	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS96058.1	7.76e-111	7	476	131	615
SDT51451.1	4.25e-102	7	471	129	592
AZN43054.1	7.83e-100	7	471	136	613
QHW34780.1	1.73e-97	7	471	134	611
AOS71572.1	1.06e-93	7	454	133	600

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PYS_A	1.17e-06	92	222	200	346	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]
6JE8_A	1.94e-06	90	192	163	278	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]
3RCN_A	3.70e-06	14	210	154	350	CrystalStructure of Beta-N-Acetylhexosaminidase from Arthrobacter aurescens [Paenarthrobacter aurescens TC1]
6EZR_A	5.31e-06	84	178	336	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]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003934_00409.