CAZyme Information: MGYG000001835_01493

Basic Information

• Species: Phocaeicola sp000432735
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp000432735
• CAZyme ID: MGYG000001835_01493
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
665	MGYG000001835_16|CGC2	76148.28	6.215

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001835	3299974	MAG	Denmark	Europe

• Gene Location: Start: 53757; End: 55754 Strand: +

Full Sequence      

MKHLILVGMVWLCSLVSVVAQSVPQVIPALQQWQPAKGKLVLPESGKVIVSSDEEGILKQ
SAEILVQDLKEMFGWNYRVVVGKKEKGAVYLTLSKPDKTLGDEGYRMDIRNGITIEAPTS
KGVFWGTRTLLQMIHNQPEGLMKGLATDFPLYPNRGFMIDVARKFFTMDYLRDYVKILSF
YKLNELQVHLNDNGFVEFFGNDWNKTYAAFRLESERYPGLTAKDGSYTKAEFRDFQKMAA
TYGVNVIPEIDVPAHSLAFTHYNTRLAADNKAYGMDHLDLYKKEVYDFVDSLFDEYLSGE
DPVFVGPEVHIGTDEYNVNESEQFRRFTNHCMDLVAKYGKMPRLWGSLKIMKGETPVDLK
GKVVSAWNYNWMDVNTCLEAGAKVVNLCDWLLYLVPAVNYYHDFLDYQWLYESWMPEMMR
KDDPKVEKRNPNFLGAMLAVWNDRVGNGISQQDVHARTFPALQVVCEKMWKGENVQHVSY
AQFEALCQSTPEAPGVNLLAKVPRRTVLMDTDKEITLSGTDVVTTSVDEIGYPYAVEFEI
CPDSIPNIDAVLFKGPHSEFVTNWQNTGKFAFRRDGYEFVFHAYRLPESKWTKVRVEGDV
KGTSLFIDGQLQERLEGRIGEVFNAKSQKKDRIWYQETLIFPLKQLGDTQMGFKGKMKNV
VCIPR

Enzyme Prediction     

No EC number prediction in MGYG000001835_01493.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	145	472	1.2e-67	0.9792284866468842

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.41e-120	153	472	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.
cd02742	GH20_hexosaminidase	6.12e-41	155	471	2	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.
cd06568	GH20_SpHex_like	8.64e-38	152	479	1	323	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.
pfam00728	Glyco_hydro_20	1.54e-36	152	470	1	343	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	1.69e-32	152	470	1	342	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
QNL40659.1	0.0	2	664	3	663
SCV07807.1	0.0	2	664	3	663
ALJ48397.1	0.0	2	664	3	663
QGT73121.1	0.0	2	664	3	663
QRQ55239.1	0.0	2	664	3	663

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JQF_A	3.96e-85	24	657	89	726	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4C7D_A	1.18e-30	25	367	8	349	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]
3GH4_A	1.21e-30	22	385	37	411	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]
4C7G_A	2.88e-30	25	367	8	349	Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1HP4_A	1.19e-28	25	367	26	367	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	5.87e-89	24	657	111	748	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
B2UP57	8.00e-26	99	476	54	453	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
P13723	1.98e-22	18	481	16	479	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 SV=1
P49008	5.50e-22	26	315	37	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q54SC9	8.51e-21	91	481	94	487	Beta-hexosaminidase subunit A2 OS=Dictyostelium discoideum OX=44689 GN=hexa2 PE=3 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
0.000253	0.999092	0.000188	0.000162	0.000152	0.000144

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001835_01493.