CAZyme Information: MGYG000004230_00481

Basic Information

• Species: Clostridium sp900759995
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900759995
• CAZyme ID: MGYG000004230_00481
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1876	MGYG000004230_8|CGC1	207648.52	4.3771

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004230	3516057	MAG	United Kingdom	Europe

• Gene Location: Start: 45603; End: 51233 Strand: -

Full Sequence      

MKQKKKQIFSFFLAFAVLLSSLGIQNINVKAADTNVASGKNVTVSSVENQLPGNVGGNVV
DGNSDTRWSSNAMKGSGANDSTTQTAQWLTIDLESERTNASEIRVAFFMKVWAAKYRIET
AATADATEWTLVKDIEQRNMGSLPDNHIDIFAGTYELQRYVRFYFDKVNPSAGGTGVSIR
EITIMGTPVVEEPTNVALGKTARASSVESALPDNVAGNAFDGSADTRWSSNAMKASGAND
DTVQTPQWLMVDLEAEATKATEISVSFFRKVWAAKYRIETAATSDATEWTLVKDIPQRTK
GSLSDDHVDTFSKEFTLQRYVRFYFEKVNPDAGGTGVSVKNITIMGRQTGVITPGTPQEP
EDELVPTYSRNFTDGNVDGVEMLYGSGATITGSSNGMNLTYTSTRAGVVDKNMTPVSDAI
YEATIVPNENGARFGLIMRATDANHKVLVGTENSNNKWFWEFWGDSGNSWGSTVTGPALT
VGKETKIKVELVGKKVTLWVDGTQVFSQTMSGTPHMANGYFGFDKTNSAGNYTIKEMKVT
AINSASSILHGINSLPTIGLDTTKVELPEVEEGYNIKIIGSNKEQVISNDGDITSHNIGD
RNVKLLVEVTNNEDEADTARRNFDVVVPSKNSKYPEIFKTVIDANEKPVIIPSIQEWYGY
NGTFTLNSNSKIIINDVANVGLRSVAENMQTDLEEITGLTIPIVIGTEGGSNDIYIESLN
EDTYGVGDEGYFMTVDEEGIKIYAHTYTGSLYGTITVEQILWRDDANKNVPYGVVRDYPD
YEIRGVMFDVGRIPHRLQYLQDYTKILTWYKMSEFHLHLNDDFEYNKDGLSTKTNTTWSG
LHRLESDVYPSLTAKDIYTGEAFEYFNNDYADPFYTKEEYRQLEDLANSRGIDLIAEFDT
PSHSTAYIEYANENPDNIEWLGPINTTVSSASNNREMLALDVNSSNQVEKQHAINARRFI
EELYGDYLGGSNPVFKSDTVHVGADEYWDKSNPEAFRQYINFLSELMASYGKTARMWGAQ
KLFPGTTVIDPANIVIDIWATYEDDPYARLAEGYQVVNVPQPYLYTTPGRDHKDMIGEEY
LYKNWDPTIFNGDIRAEAGEPLLLGAKAALWGDEFREGITEADLHERMLRSAAMVAEKTW
GGQSEEDSYIEYQKAFEDLEEGPGTKIAHTIISESEVVVDYDLQETINSNSNIVVKDASG
NGYDAVVENGKIVDVDGTKMIKFDGTTKMTTPLETLGYPYTVSFDVKASDGNNKDSLLFS
GYDGQLLAKGISNSFMTVRRSFYTQPTGFELPTDDTANVTIVGTFQNTKIYVDGVLVKML
YSADDGNSSNYWSTFVFPMKEIGLNFHGYMGNIKAYNKALQPEMIRNAADMTEINVALNT
EAYAERFGGSPALNSGDLKRHPAWKATDGDKNDLASTIISTDPNSYWLSSNNNNDYLMVD
LDEVKDISKVVITWNGTQYATSFRIETSIDGKNWTTVETISGNTASENTITLATPVEAQY
VKVQGITRNANYYGIREVEVFEKVDKSPLKAEIADVKTVIVRDKLETSEMQQAKELMRAL
ITAEKMLNNPFTTTQIAAVEKSKLASALSVYNNAKEQPEVVDKTVLRLVIDYAEEVKAGG
ALENVVPSVVTEFEAALQEAKAILADANATEVQIDLAEKRLINVIHMLEFKKGDKAELAK
LVEIINALEENKYTVSTWAALQAELAKANAVIADENAMEAEVTKAYEDLNKEFSNLEMVV
STDKAKLQQLVTELEGKDTSKFTSGTVAKLNSELANAKAVLENKEATQEEVDKAVEGLEL
ALNNLELAQANDNEKPVENPVNKDDNKDPGDVNNPEDIENSPTTGDTSYVFLYVGFMIMA
CVALYILKKKNRYQNQ

Enzyme Prediction     

No EC number prediction in MGYG000004230_00481.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	777	1141	3.4e-52	0.9673590504451038
CBM32	1399	1518	1.5e-22	0.8629032258064516

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	5.90e-79	782	1142	1	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.
pfam00728	Glyco_hydro_20	1.33e-37	781	1140	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	4.37e-35	783	1141	1	303	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	4.60e-31	662	1149	141	622	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06563	GH20_chitobiase-like	7.67e-26	781	1147	1	349	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
AXH51903.1	1.36e-230	191	1527	38	1274
QQA11576.1	2.77e-229	191	1527	38	1274
ASY50997.1	3.87e-229	191	1527	38	1274
AWS25495.1	3.87e-229	191	1527	38	1274
AMN35076.1	5.84e-227	192	1526	39	1273

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	2.40e-57	554	1362	8	733	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
3GH4_A	5.68e-23	644	1140	35	490	Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
2GK1_I	6.03e-23	729	1154	26	411	X-raycrystal structure of NGT-bound HexA [Homo sapiens],2GK1_J X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_K X-ray crystal structure of NGT-bound HexA [Homo sapiens],2GK1_L X-ray crystal structure of NGT-bound HexA [Homo sapiens]
2GJX_A	1.16e-22	729	1154	92	477	Crystallographicstructure of human beta-Hexosaminidase A [Homo sapiens],2GJX_D Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_E Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_H Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
7BWG_A	1.25e-19	729	1140	87	476	AGlycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5],7BWG_B A Glycoside Hydrolase Family 20 beta-N-Acetylglucosaminidase [Microbacterium sp. HJ5]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	2.69e-60	554	1362	30	755	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
P06865	7.53e-22	729	1154	114	499	Beta-hexosaminidase subunit alpha OS=Homo sapiens OX=9606 GN=HEXA PE=1 SV=2
Q5RC84	1.77e-21	729	1154	114	499	Beta-hexosaminidase subunit alpha OS=Pongo abelii OX=9601 GN=HEXA PE=3 SV=1
Q0V8R6	5.50e-21	729	1143	114	488	Beta-hexosaminidase subunit alpha OS=Bos taurus OX=9913 GN=HEXA PE=2 SV=1
P29416	7.00e-20	729	1140	114	484	Beta-hexosaminidase subunit alpha OS=Mus musculus OX=10090 GN=Hexa 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
0.000216	0.999097	0.000187	0.000171	0.000158	0.000140

TMHMM  Annotations     

start	end
7	29
1848	1867