CAZyme Information: MGYG000000765_00307

Basic Information

• Species: Porphyromonas_A bennonis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A bennonis
• CAZyme ID: MGYG000000765_00307
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
647		73401.33	5.1417

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000765	2007181	MAG	Bangladesh	Asia

• Gene Location: Start: 40359; End: 42302 Strand: -

Full Sequence      

MNKPFLLLCLALASVSSVFAQESRYKDITPRPLLAEQHSGAIPPDFALIPQLSSDSLSTL
TPAIDRAFPRRAGHEVTLSLRCTDTLSFSPSVEAYRVLVSPSEVLIEGRSIRGVYNGIQT
LRQLVSDSGIPCGVVEDAPAFRWRGFLADVGRNYQSVVLLKQQIDAMAGLKLNVFHFHAT
EDVAWRLESRLYPVLNNPSTMTRDKGLFYRYEELEELRRYCEERFILFLPEIDMPGHSAA
FERAMGCSMQSEKGQAIVMELLDEFLSHVDCPYLHIGADEVKIHNRDFVPTVVSFIEAKG
VKAIGWSPGGNYPETVIRQLWSAAEKSEIDNPKVAKIDSRNLYINHMDPLESVVSIFYHS
ILDSDSDNNDEHLLGGELCLWNDRNLLYGDLNHVHNPTYPSLVAFAEKGWGGGGYVDNFV
SLSQNRDFECFRDFERRLCIYGKRYMQGLPFPYMPQSEIRWSIFGPYPNGGKTAMAFPIE
ALSPEELESLTPDTTFIGGTLILRHFWDPQIKGLWIDPAPNQTVYAYRRVWSDEERESSL
WIGFYDYSRSQWADAFPKGKWSNTDAQIWLNGETIAPPLWAHSGQKGDPEIPFWDENYTM
RTPTRVTLRKGWNTLLLKIPAGSFVGSAWYAPVKWMATAVFVDDMLQ

Enzyme Prediction     

No EC number prediction in MGYG000000765_00307.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	136	411	6.3e-51	0.9703264094955489

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd02742	GH20_hexosaminidase	9.40e-64	143	411	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.
cd06563	GH20_chitobiase-like	7.33e-42	141	438	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	1.48e-37	141	410	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06568	GH20_SpHex_like	3.77e-36	141	438	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.
cd06570	GH20_chitobiase-like_1	8.10e-33	141	410	1	296	A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase 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 subgroup 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
AYD48368.1	5.94e-198	93	644	309	861
ALL08794.1	4.69e-186	93	645	104	656
QEC70712.1	4.05e-185	52	643	294	882
ATP56422.1	1.42e-181	93	640	105	650
QEC54485.1	6.98e-180	93	643	309	855

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PYS_A	4.00e-30	93	419	78	470	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]
6YHH_A	1.64e-29	93	417	92	483	X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7DUP_A	5.51e-29	93	280	79	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
3GH4_A	6.84e-29	93	414	122	494	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]
7DVB_A	2.38e-28	93	280	79	316	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49008	2.19e-29	93	455	111	540	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7WUL4	1.41e-24	28	313	6	335	Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
B2UP57	1.92e-22	93	244	58	221	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
P96155	6.18e-22	64	281	151	436	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
Q8L7S6	7.76e-21	83	410	113	484	Beta-hexosaminidase 3 OS=Arabidopsis thaliana OX=3702 GN=HEXO3 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
0.000282	0.998965	0.000227	0.000169	0.000166	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000765_00307.