CAZyme Information: MGYG000003963_01389

Basic Information

• Species: UMGS1696 sp900753285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900753285
• CAZyme ID: MGYG000003963_01389
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1803	MGYG000003963_15|CGC1	196574.62	4.2446

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003963	2551706	MAG	United Kingdom	Europe

• Gene Location: Start: 28114; End: 33525 Strand: -

Full Sequence      

MKQLRHVLALTLVFCMVFGMVTPSLAVSGEISVEEDYGIPVEEDGGIEIEVDDRSDYDID
EDREELSVLPKQDETADETNTTGKVDGYNYNIIHLDCGRKYFSVDSIKQIIDNASAAGFN
YIQLAVGNDGMRFLLDDMSLTVNGTTYKSKEVSDAIHAGNVAYNESAKYNNKAYVTDVNE
LTQSEMDAIIKYAYEKGMGVIPLINTPGHMDAILDAAEALTGKTCSYNGSVRTIDVTNTT
AVAFTEAFLNKYITYFAGKGCTLFNMGADEYANDIYTSGSMGFGNLQSSGKYSYYVTYVN
EVATLIKNAGMKPMAFNDGIYFNNNTWSVTFDTDIIIEYWSNGWSGYTPMPASELAKDFA
MVNTHGDYYWVLGKPDAQCSATKASGFDKTVFPGSTISNPGGSTFCIWSDYPGAETEASV
ISKTADTIEAFGGTLPTVDSVTNGGTTDPVGKTVEITLNVGESTTRTINGAAVNKTIDDN
VAKVVAVGASVAGETTYTLADTIVSGNKYCISDGNGNYLSVNSEGGILNRKENDSPDKSP
TEWTIKGSGSSYTIKDETTGYYLCYKNSQLNASKTSYDRYWNYDQSGFNVTSYGNTYYIR
SYNNDTWYLAYWSSNHGLPYTKTTTTAETKTSVTITGKAPGYTTAIVGGVTYNITVNAIE
ETKSLTVSSGNTAALDVPALDESIVGNTTTTYDVTIGSDYITVDKTNGTITAEIVTEDKT
ATVVAKVKKAGGIVLATYTYNVTITKEDLDKVTPITVEYWITNSRLTGETSKENQVTITA
QEAFGEGGVDIVAKVDPEGNKDNRTQEYWQSKILDVEKTNNSTSGTELQTTKKGDDETLN
GSAFTKIRYYNSKWQVYTTKWTDVDRTQVSFKYTGDNSTTVTYSGDKNQLVAYYMEVVNI
NNANNESELHVNAADWGTKGDGTGSWGYTPESNRCSVSVQIVYEDGSTNPSDTTATNLKS
KTIMYGYWDGGRGLGTMIFSGQQNYQIYKVTAETGDVTSTTGSGNTVTVTNFTWDENEET
VWEGDATKSVSIGNPARNPSYVAPYDNLAWNTTKYNKNNAILIRVYVKTGVTEDSLTVHY
IDKTLNEEFYNYNIAVASGTYFDSAFGKGGGNTLVNNSVKNINGVTQSVNADLTTMPEIS
AYYRYSEFTLDSVKRSDNGKEVWLYYTFNNTHNFVVDFGVPLHLEPSDIGIGETSGTQKW
DTAELTAGNKLIYGTVDIAVGEGLTYTPTSVMKGVETIGITLSESNSTAKPATHFIYLYP
ATNVLYEENVITNPGTEWTTVTSVFTPATDEKGNITTQSAEKLGEENLHGYDNYYSENTE
FSGGSAYMATLDASKTATEIGKPLTFEFTGNGFDLISECGPQTGALLVRVYKDGVLNHGF
FVDTYFTGDNIGIINSAADNNGVLDYQVPVVRDINLTHGTYKVEVYGYMVNRSTTSTASL
YSVDSAETYLEQALRDLGLDDDTSLYEVSFMDENSVLNDNAVASDVVRSGVSVQSMANDV
MAETDATQYVYVDGIRVYHTIDAAAEPEYTASEQDVTYYDIYDIAKKSGMTIGSYLVYVE
GEGNRATLENYHNKGPQNEIYLTSGNTLAFKLDGYTENQINLKSIQISARAVTEEAAFVD
NGKPIPIATNTEMYYSVQLLTTSDTKEYYLSIKCPKNTDGTNSMLSIGAIKLPNGVTIAE
ATESVKADVLRRAKAQDSDEFIPSSFTVNVAESVKAGKRFYLGAQTSIDVDKLIVEYQGV
EYEITPDNAELVSRGVADVYTYSSGFKAPKRGVADSVTVTVKAHKAGTDDVYSTPVTYTV
VVK

Enzyme Prediction     

EC	3.2.1.52	3.2.1.96

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	84	416	2e-41	0.9109792284866469

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.07e-68	90	445	2	326	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	4.52e-19	93	411	4	279	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.
COG3525	Chb	3.66e-16	93	405	430	694	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
COG3525	Chb	1.56e-15	96	347	18	259	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06562	GH20_HexA_HexB-like	1.61e-12	95	411	8	300	Beta-N-acetylhexosaminidases 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. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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
ALP95510.1	8.43e-142	86	1664	116	1691
QBB67228.1	1.26e-117	86	1638	116	1661
QPC25106.1	7.30e-85	66	426	23	368
QEM96726.1	7.30e-85	66	426	23	368
QDR74992.1	7.30e-85	66	426	23	368

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7PUL_A	7.44e-79	91	427	11	341	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
4AZB_A	1.62e-68	92	423	9	352	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZ7_A	2.90e-68	92	374	9	294	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	2.98e-68	92	374	9	294	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZ5_A Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZ6_A	3.06e-68	92	374	11	296	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49610	3.08e-62	92	374	189	474	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 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
0.000381	0.998831	0.000244	0.000171	0.000175	0.000163

TMHMM  Annotations     

start	end
7	29