CAZyme Information: MGYG000004436_00312

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696
• CAZyme ID: MGYG000004436_00312
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427		50030.61	6.0288

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004436	1421600	MAG	Israel	Asia

• Gene Location: Start: 1153; End: 2436 Strand: -

Full Sequence      

MRLEDLTLLTPAKTPGDTQWFRHDRFGMFIHWGLYALGARHEWLKSHDRIPTEVYDKYFR
HFDPDLYDPEKWASAAADAGMKYFVITTKHHEGFCLWDSAYTDYKSTNTPYGKDILTPMV
DAFRSHGLRTGFYHSLLDWHHPDYTVDICHPMRDNEEYIAEDKNRVLSRYVDYLHNQTEE
LLKRYDPVDILWFDFSVGASDKFPGKGKEVWRSAEFLEKIRAINPNIIIDDRLQIDQDVK
TPEQYMPDEWVKVNGVPVVWEGCHTFSGSWGYYRDEESWKSVDQLLKMLIDSVSMGGNLL
LNVGPTGRGEFDERAYDRLAGIGKWMRRHSRAIYGCTQAPLEFVCPRDCRYTYNPETKRL
YLHMYSWPFGKITLNGEVAEHVEYIQILSDASELPFTYDAENRRVHIPLPVKKPLGADIP
VLEIYLK

Enzyme Prediction     

EC	3.2.1.51

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	16	335	2e-103	0.884393063583815

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01120	Alpha_L_fucos	8.93e-109	19	329	20	331	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	1.98e-103	19	374	21	381	Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
COG3669	AfuC	1.28e-34	18	335	12	321	Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOR34951.1	2.29e-217	8	427	1	429
ACX65312.1	1.33e-208	13	427	7	433
ANY70321.1	1.15e-196	11	427	18	450
AFH63261.1	2.49e-194	14	427	8	434
AEI43281.1	2.49e-194	14	427	8	434

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6GN6_A	1.97e-120	19	394	32	407	Alpha-L-fucosidaseisoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_B Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_C Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_D Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_E Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus],6GN6_F Alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus [Paenibacillus thiaminolyticus]
4PCS_A	7.31e-72	19	414	20	425	Crystalstructure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_B Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_C Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCS_D Crystal structure of a bacterial fucosidase with iminosugar (2S,3S,4R,5S)-3,4-dihydroxy-2-[2'-phenyl]ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_A Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_B Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_C Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],4PCT_D Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482]
2WVT_A	8.13e-72	19	414	24	429	Crystalstructure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVT_B Crystal structure of an alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron in complex with a novel iminosugar fucosidase inhibitor [Bacteroides thetaiotaomicron VPI-5482],2WVU_A Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_B Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_C Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482],2WVU_D Crystal structure of a Michaelis complex of alpha-L-fucosidase GH29 from Bacteroides thetaiotaomicron with the synthetic substrate 4- nitrophenyl-alpha-L-fucose [Bacteroides thetaiotaomicron VPI-5482]
4WSJ_A	8.56e-72	19	414	20	425	Crystalstructure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one [Bacteroides thetaiotaomicron VPI-5482],4WSJ_B Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one [Bacteroides thetaiotaomicron VPI-5482],4WSJ_C Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one [Bacteroides thetaiotaomicron VPI-5482],4WSJ_D Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one [Bacteroides thetaiotaomicron VPI-5482]
5I5R_A	8.79e-72	19	414	21	426	Crystalstructure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],5I5R_B Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],5I5R_C Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482],5I5R_D Crystal structure of a bacterial fucosidase with iminocyclitol (2S,3S,4R,5S)-3,4-dihydroxy-2-ethynyl-5-methylpyrrolidine [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q99KR8	9.18e-43	20	411	43	441	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q6AYS4	6.32e-42	20	397	41	426	Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
P17164	6.67e-42	19	399	47	431	Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1
P48300	7.02e-42	20	408	52	444	Tissue alpha-L-fucosidase OS=Canis lupus familiaris OX=9615 GN=FUCA1 PE=2 SV=1
Q5RFI5	1.35e-41	20	368	47	401	Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004436_00312.