CAZyme Information: MGYG000003295_01321

Basic Information

• Species: CAG-312 sp002437405
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312; CAG-312 sp002437405
• CAZyme ID: MGYG000003295_01321
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
512	MGYG000003295_222|CGC1	58102.31	6.6587

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003295	2127186	MAG	Mongolia	Asia

• Gene Location: Start: 10374; End: 11912 Strand: +

Full Sequence      

MKIAELLSAAAISVLPLFAYSAQPVSDTVRNIMDERLAPKPVSTAYFEGLYNLSDKSAVS
VETPAKLTDEQKSVILKTFKDYWKLSPNVVFTESDSATAIKREGYNLDIAPQGLKISAKD
FEGVRHALKTVRQLAEVGRDNDGYFLQSCKITDAPALDFRAVHLCIYPETTPAELEKRVR
LAAYYKFNYVIIEPWGTFPFKTHPELSFNNKTFSRVELRRIIDLAYELGITPVPQLTILG
HVSGGTNESAKHAILTRFPEMAKLLEPHGWSWCMSNPEAVKLLEEAVAEIHEFFGNPPFF
HIGCDEAYDMATCYKCRQTSLGKLLGKHILHFRNLLEKRGARTIMWHDMLVEEGDPRWDK
CTATGHPNTDMNELFKALPKDVVIADWQYDPLPKGQKYWPTSIYFKENGFDTLICPYFEI
SNIKNAEATACDNKLFGMICTTWSRTMGSPGRRLFYTAANAAWGSDPKKFSNSWKDFRCN
YNTHLRTMDIDSDIDNYEDLGSTPHVGVERHL

Enzyme Prediction     

No EC number prediction in MGYG000003295_01321.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	171	416	3.1e-25	0.6735905044510386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	2.31e-31	159	445	1	278	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.
cd02742	GH20_hexosaminidase	5.40e-10	171	350	14	194	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.
cd06564	GH20_DspB_LnbB-like	6.95e-10	160	411	3	237	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.
cd06563	GH20_chitobiase-like	2.08e-09	213	478	83	354	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	1.32e-08	213	388	65	224	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
BBD46391.1	5.17e-112	30	501	45	517
ASV74378.1	6.52e-54	143	443	235	534
AXA35531.1	3.88e-26	37	423	284	673
CCW34388.1	9.00e-26	103	471	334	704
AQQ70534.1	7.10e-24	37	444	300	722

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	6.38e-07	188	350	31	193	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2

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
0.000678	0.998515	0.000246	0.000188	0.000180	0.000172

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003295_01321.