CAZyme Information: MGYG000004314_00014

Basic Information

• Species: Varibaculum timonense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum timonense
• CAZyme ID: MGYG000004314_00014
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1392	MGYG000004314_1|CGC1	149480.75	6.2119

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004314	2027678	MAG	Israel	Asia

• Gene Location: Start: 29620; End: 33798 Strand: -

Full Sequence      

MFNRSKKVFCLLGAGALALAALLPAGIGTAEAAEPTNHALAAKGGSVSASGNEVADKWQA
QAAIDGNDSGDSRWSSNHSDQAWIAVHLKEAIKIDHVTIKWEAACAASYHLEVSTDGTTW
EKASDTIRPQCSSTDTQKLNAATANGTWKYVKMQAESRTPFQGIKYGVSLFEFEVWDGAE
PVAPAQPNLIPLPAEMTPGEGGFELGADTKIKTDSASKAIAEMTAKTMRASTGFPLPVGK
DGQISLRVDTGLDTTGLTSGNIEEAYSLKVSESGVEIVGKSPQGVWNATRTLLQLFPAFI
YSPHQVNSQWLAPAITVKDAPRFAHRAIQADVARSFLTIADLKQMIDTFANVKGSRLHLH
LSDDQGWRLQITNEGREAGDTIDYSRLTEVSGKTAMNWNSEAYSLKDLTGSSQQADDNVV
ELGHHGSYTQEEYKELVKYAAERFVTIQPEFDMPGHTNAALSAIPQLNSAKSSHNGTVDA
DGNAITDPAKWQVAPANGTGDVGYSYLDPDSKHTQYFVRHVFKQLAALTPGKIIHIGGDE
SHDMVTKLGKDKFNEFLNMSAKAVRDQGKSPIGWNEIASNTLQPGDLVQYWTGSTANTKR
AIQNEGVKVAVSNASTAYIDMKYGVPGGNSIGLTWSGTGDFDKYYNWDPAQVIKGIPESS
IVGTVAVQWSETIRGGYQAEWLMWPRSISHAEVAWTPQAKRNVNQFKQRMAAMGDRLAVS
AVNFFDGPKANWQTALAGVDQKVAPGRSVNLAVGEFAAPGTVKNSEGTQITKADNAASAL
GDTPFSATIDWGDGSAPSPAIFTQSHSRDALHSSPLYKVTGKHPYANPGTYTGTITGSNG
QKTTFTVNVANGAPDPSENNPWDASKKPTITIEKNLIRPYERVKVKLSGFEPGKYVKLAW
NGKTQFLAMPGADGSAEYYLPFFDKAEKVLRPQDSGTHQLSATQIGANRSAEVTATIVSN
REELLNPVAQCPTMNDPNCGYENITASSQADNEPKPSGPVSAAFDGDPNTYWHTRWAAPA
GTFPHTVTAQLKATPEQKCVITGFEYTARSGQENSRVKDFRIEVSENGKDWKSAITASLK
NHADPQVFNFAADKQLSGKYVRMVQLNSQAGNDFGGAAEIRFGAVCAQNGTEVTPVAPVA
EKQPLTAQGKEYPGYFLVPLVTGVNYYLGDGLLTPQQAVPLPFGKTKVVAKPASDLFRFK
EGAKSEWILDMGEDPGQVEPPQPEKPEKPAPQVVKGDWTDSSGQDASNCKTFKVMQTRSV
TTTEYIWDATGAKWVLDTANAQVTTEQGVRDMSAAEKEKCAASPEEPSPDNPSLDKPGKP
DGQPDTKPGTGSDNGAVKPGNTGSKPDAKPRQQNTTSAMPSTGASSELSLLLAALSIGFG
GVLLLSRHRTRR

Enzyme Prediction     

EC	3.2.1.52

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	318	698	6.6e-81	0.9762611275964391
CBM32	49	174	7.4e-19	0.9354838709677419
CBM32	985	1119	6e-17	0.9516129032258065

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06568	GH20_SpHex_like	9.65e-121	323	710	1	329	A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. 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. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
cd06563	GH20_chitobiase-like	6.37e-77	323	710	1	357	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.
pfam00728	Glyco_hydro_20	1.31e-72	323	697	1	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742	GH20_hexosaminidase	1.47e-55	325	695	1	302	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	6.97e-51	178	731	125	649	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQO77161.1	7.94e-309	3	1131	9	1118
QGH68632.1	3.43e-302	13	1130	15	1113
QQM67569.1	3.31e-300	14	1132	16	1106
VEG55568.1	3.86e-286	4	1135	11	1109
AVM62491.1	2.71e-271	113	1126	1	984

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HP4_A	1.20e-82	183	732	17	511	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]
1M04_A	5.69e-82	183	732	17	511	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1M03_A	1.45e-81	183	732	17	511	ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
4C7D_A	1.07e-80	188	732	8	493	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
4C7G_A	2.71e-80	188	732	8	493	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7WUL4	4.83e-66	189	732	6	485	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
P49008	1.01e-58	188	724	36	532	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6	7.07e-49	169	724	13	529	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
P96155	1.47e-36	188	686	140	596	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57	1.71e-36	194	711	2	463	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

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
0.000256	0.999048	0.000160	0.000210	0.000158	0.000137

TMHMM  Annotations     

start	end
7	29
1368	1385