CAZyme Information: MGYG000001903_01040

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales; Firm-18
• CAZyme ID: MGYG000001903_01040
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469		54830.55	4.6376

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001903	2217690	MAG	Denmark	Europe

• Gene Location: Start: 10; End: 1419 Strand: +

Full Sequence      

MIETGGALEYKKHPEINEGWEEYCRIFNEYQGKTIDVQKSCGWMKNSIHFENGGGSWLTQ
EEVSKLVDFCRKYYMDVVPEIPTLSHSDYILTRHPELAERAEDPLPNTYCPSNPETYKLI
FDIFDETIEVFRPTAVNIGHDEYYDICLCEKCRKKDAADIYADDVNKIYKYFKDRGIGVA
MWGDKLLNVITKAGYHYGGSQIEYDTADGRHYTVPATYKSIEKIPKDITIVNWYWRIDRK
LDKVYFENGFENVLYGNFKPMQIYDCRERMDGKISGYYISNWSSLDPAHIQRNGIFAGIA
YAAAMFWKPDFCENEFESNFINMSNDIFCYNYNIANPGNYACVVHTTSETRPHKEFVDGY
LMDYDGDYLGEYTVYYTDGTTDTQKLWFGLNIGNCDVKIGTKPWYDSDCYELLPYFYEPG
FTCAYVPADEKMYYRYMLKVDGSKQVKDIKLTDGNVEVREIKYDNRDFT

Enzyme Prediction     

No EC number prediction in MGYG000001903_01040.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	13	256	9.4e-33	0.5667655786350149

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	3.13e-28	58	234	57	211	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.
cd06564	GH20_DspB_LnbB-like	7.66e-19	54	184	75	201	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	1.74e-14	51	194	68	231	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.97e-10	59	176	84	218	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.
cd06570	GH20_chitobiase-like_1	2.67e-09	54	142	61	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZN43054.1	6.95e-128	1	462	165	646
QHW34780.1	1.29e-124	1	463	163	645
AUS96058.1	2.75e-123	1	439	160	615
SDT51451.1	6.85e-120	1	402	158	559
AOS71572.1	3.81e-112	1	455	162	639

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6Q63_A	2.43e-11	3	186	200	392	BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
6YHH_A	2.97e-07	55	142	205	317	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]

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
1.000083	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001903_01040.