CAZyme Information: MGYG000001905_00585

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; Firm-07
• CAZyme ID: MGYG000001905_00585
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
642	MGYG000001905_7|CGC1	73594.76	5.8194

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001905	1626943	MAG	Denmark	Europe

• Gene Location: Start: 27467; End: 29395 Strand: +

Full Sequence      

MKNQIYFSGLPAAWKESAQSLLFDLGIGLSKEGTKVTVTSGDGLDICRTEDGIRLAVKRQ
QDFSRALSYLPAFLSGRKTAVFEKCNANTLCLMADCSRNAVLSMDGAKKMIRDLAVMGFD
SLMLYTEDTYELPDYPYFGRQRGRYTVSELKELDDYAFSFGIELIPCIQTLGHLERALQW
KAFDGMKDTDDILLVGEEKTYALIDEMLRVYASAFRSRRVNIGMDETHTLGRGKYMDLHG
SRKTSDIMLEHLGRVNELCRKNGFAPMMWSDMFFRMAFNGRYYISEGEISKEVMDKVPEG
VTLIYWDYYTSESQRERFSHMLDCHRKFPHNKTAFAGGAWCWAGFTPHARFSVNSTRIQL
EECRKRGMKDFIVTAWGDNGRETSLYTTLTTLLLYAEYAYTGELPDNARLESRCRDTFGI
GFEELLTLDAPDAMAHRGDTELVHPRNPSKYLFFNDPLEGLRDAHMDPENVSADFADAEK
QLRKYENHPRFGYLYRSLADLCHVLIRKADFTVRLRGAYLAGDRDRIAVIADEVPLIISD
IERFLESFRAQWKKENKPAGFLVQELRIGGLIQRMKGAELRIREYLAGEADTIPELEEPV
LPFNGKNETSPYTTNEDFVMKGDSTPYFYDNIWHRIVTSCIL

Enzyme Prediction     

No EC number prediction in MGYG000001905_00585.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	92	402	7.7e-39	0.9436201780415431

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06565	GH20_GcnA-like	1.98e-102	93	380	5	280	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.
pfam18088	Glyco_H_20C_C	4.92e-56	423	605	1	184	Glycoside Hydrolase 20C C-terminal domain. This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature.
cd02742	GH20_hexosaminidase	6.54e-39	90	382	2	282	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	1.28e-11	92	309	5	224	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	2.98e-11	92	273	6	223	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV34232.1	8.09e-151	1	642	1	628
QCJ40720.1	1.35e-148	54	642	53	626
AIQ36288.1	8.09e-148	1	642	1	628
AIQ74915.1	9.07e-147	1	642	1	628
AIQ24479.1	9.07e-147	1	642	1	628

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2EPL_X	4.71e-131	7	639	4	621	N-acetyl-B-D-glucosaminidase(GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPM_X N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii [Streptococcus gordonii],2EPN_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPN_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_A N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii],2EPO_B N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii [Streptococcus gordonii]
5A6B_D	1.23e-130	1	639	21	642	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5A69_A	1.97e-129	1	639	21	643	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-PUGNAc [Streptococcus pneumoniae TIGR4],5A6A_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6A_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with NGT [Streptococcus pneumoniae TIGR4],5A6J_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6J_D GH20C, Beta-hexosaminidase from Streptococcus pneumoniae [Streptococcus pneumoniae TIGR4],5A6K_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5A6K_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with Gal-NGT [Streptococcus pneumoniae TIGR4],5AC5_A GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4],5AC5_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GlcNAc [Streptococcus pneumoniae TIGR4]
5A6B_A	1.97e-129	1	639	21	643	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4],5A6B_C GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with PUGNAc [Streptococcus pneumoniae TIGR4]
5AC4_A	5.51e-129	1	639	21	643	GH20C,Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4],5AC4_B GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A6QNR0	5.29e-10	117	361	28	261	Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q8WVB3	2.13e-09	117	308	36	225	Hexosaminidase D OS=Homo sapiens OX=9606 GN=HEXD PE=1 SV=3
Q3U4H6	1.98e-08	117	308	36	225	Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd 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
1.000026	0.000019	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001905_00585.