CAZyme Information: MGYG000000592_01216

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9
• CAZyme ID: MGYG000000592_01216
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
256		28353.58	6.2334

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000592	2977283	MAG	Madagascar	Africa

• Gene Location: Start: 5777; End: 6547 Strand: -

Full Sequence      

MKQQVKELMTQYAPVRALWFDGYWDHKRDSIPFNWKMPEFYEYIHSVDPACLIGNNHHIQ
PIEGEDFQMFERDLPGQNTAGYSEGQMVSDKLPLEMCQTMNHTWGYSVSDRDYKTAAQLV
GTLAKAVSMNTNLLLNIGPRADGRLPDAALALLKEIGQWMKVNGESIKGCGPGPVAEQEW
GVTTAPLAGGKTFYIHVLQNPGAVLEIPVAKKSKVKTVTALSDGTTLPVKKVGEKLFITL
PADLPAEDYVVSVTMK

Enzyme Prediction     

EC	3.2.1.63

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	1	167	1.2e-46	0.42196531791907516

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01120	Alpha_L_fucos	3.48e-60	1	165	181	333	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	1.38e-44	4	201	184	374	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	1.39e-15	7	172	157	324	Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13003.1	8.36e-90	1	256	190	439
QCD43615.1	4.03e-78	1	256	171	419
QUB51464.1	2.50e-77	1	214	203	411
QUB53252.1	2.50e-77	1	214	203	411
AEE12404.1	2.91e-77	1	255	185	432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6GN6_A	3.27e-39	1	256	187	444	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	1.26e-17	4	256	178	436	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]
4WSJ_A	1.28e-17	4	256	178	436	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]
2WVT_A	1.28e-17	4	256	182	440	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]
2WVS_A	1.28e-17	4	256	182	440	Crystalstructure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_B Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_C Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482],2WVS_D Crystal structure of an alpha-L-fucosidase GH29 trapped covalent intermediate from Bacteroides thetaiotaomicron in complex with 2- fluoro-fucosyl fluoride using an E288Q mutant [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P10901	1.14e-15	1	254	203	458	Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1
P49713	1.64e-12	4	172	194	354	Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q9VTJ4	6.00e-11	1	209	209	415	Putative alpha-L-fucosidase OS=Drosophila melanogaster OX=7227 GN=Fuca PE=2 SV=2
Q6AYS4	1.90e-10	4	167	204	359	Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
C3YWU0	2.52e-10	4	241	197	428	Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2

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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000592_01216.