CAZyme Information: MGYG000002251_00507

Basic Information

• Species: RQCD01 sp008668455
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; RQCD01; RQCD01 sp008668455
• CAZyme ID: MGYG000002251_00507
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474		54678.21	4.9875

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002251	1374022	MAG	Peru	South America

• Gene Location: Start: 58; End: 1482 Strand: +

Full Sequence      

MQTLKQLLSENAEKVRCQQITDAPDMKYRGFYQDVTRGKIPTLETLKSLADTMAFYKMNS
LQLYVEHVFEFREYEFCREQLGYLTKEEIRELDRYCKTKFIDLVPSVSLFGHLYHLLSNE
KYRHLSELPDYQPTRHYWLERMQHHTINPTLEESFSVIKSLIDQYLEVSTSEYLNICCDE
TFDLGTGANAGKDKGKLYFDFVKKIITYLHEKGKTVMMWGDIILQHPEYIDQLPEGVIFL
NWGYDQNPDEEQYKKVAESGREQILCPGTSSWNAFTEHVDVEEGNISALAAYGHKYHAAG
ILNTNWGDWGNIASLSMAMYGMVLGAALAWSKETTADSAFRAEASQLLFGNRDTVAILKE
LSAIRYAADWEKVVDGHSDRIVSAEDYEKAFTLCRDCLEKVKELSFREELVKREAISAIE
GYEMMLSLCAKANGLTVSGKTSIPAWLEEYKTLWLIRNKPSELDELIRVIEKWL

Enzyme Prediction     

No EC number prediction in MGYG000002251_00507.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	24	332	4.6e-50	0.9643916913946587

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	9.09e-85	28	331	1	301	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	4.07e-24	27	255	1	234	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.
cd02742	GH20_hexosaminidase	3.18e-23	28	308	1	278	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.
pfam00728	Glyco_hydro_20	3.26e-20	27	269	2	263	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.86e-17	28	268	3	262	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS98665.1	1.20e-106	1	463	102	602
BCJ98685.1	3.58e-101	1	470	104	607
AQM60214.1	8.67e-98	1	470	105	603
QOR35259.1	3.19e-96	1	467	99	595
BCJ97085.1	1.46e-95	1	470	103	603

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1M03_A	3.94e-09	1	272	123	399	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1M04_A	6.90e-09	1	272	123	399	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
6JE8_A	8.51e-09	3	112	64	193	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]
1HP4_A	9.14e-09	1	272	123	399	ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]
4PYS_A	1.97e-07	17	249	121	368	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
A6QNR0	1.36e-10	85	249	57	222	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
B2UP57	4.86e-08	3	112	85	214	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1
Q04786	1.49e-07	1	283	290	634	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
B2UPR7	5.73e-07	3	222	209	445	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
B2UQG6	4.58e-06	20	222	144	379	Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1

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 MGYG000002251_00507.