CAZyme Information: MGYG000003424_01139

Basic Information

• Species: SFTJ01 sp004557385
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; SFTJ01; SFTJ01 sp004557385
• CAZyme ID: MGYG000003424_01139
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
450		51723.77	7.7166

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003424	2699357	MAG	Fiji	Oceania

• Gene Location: Start: 2915; End: 4267 Strand: +

Full Sequence      

MKRILLSMLLAAMLMPVVAQQRITGESKENYEKRMEWFGDAKFGVFIHWGIYAVRGVSES
WSFFNNYLPYDEYMKQTEGFTASKYNAKEWVDLIEQSGARYTVITSKHHDGFALWDTKAG
NISAKKSSAAKRDVLTPFAKEVQKRKNLRLGIYYSLLDWSRDDYPNATRTSTRYNIKEDP
KRWAEFCKFNFAQLRELNETYKPALYWFDGDWEQSAEDWNSKGIIDLLRSTNPNVIVNSR
IQGYGDYDTPEQGIPVVRPESKYWELCYTMNDSWGYQHTDKDFKTPHMLLRTLCDCMSNG
GNLLLDIGPKADGTIPQEEVDILKEFGRWIGKHKEAVYGTRAGLPAEHFPDGYTTLNKGG
DIVYLYIPNKVRGKICLRGIVNKVNRVWVVGNGSMLSYKVYDKPYWSSLPGIVYIDVPED
VQDEQITVIAVLLDGPAKLYRGHGQVITSN

Enzyme Prediction     

No EC number prediction in MGYG000003424_01139.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	21	339	2.3e-97	0.9190751445086706

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
smart00812	Alpha_L_fucos	3.27e-124	24	380	10	384	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.
pfam01120	Alpha_L_fucos	4.06e-111	26	335	11	333	Alpha-L-fucosidase.
COG3669	AfuC	8.53e-38	48	360	1	339	Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADV42531.1	1.51e-257	17	450	20	452
AVM58091.1	1.13e-252	19	450	22	452
AVM54046.1	1.60e-252	17	450	20	452
QRO24790.1	1.51e-247	16	450	19	449
ABR41654.1	2.89e-245	6	450	11	449

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6GN6_A	4.47e-72	32	434	28	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	6.57e-49	24	370	9	378	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	7.14e-49	24	370	13	382	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	7.44e-49	24	370	9	378	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	7.59e-49	24	370	10	379	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	3.92e-50	8	377	7	404	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q6AYS4	1.97e-49	37	418	41	438	Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
C3YWU0	3.18e-48	37	369	33	387	Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2
Q9BTY2	3.27e-48	37	398	49	433	Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
Q5RFI5	4.38e-48	37	398	47	431	Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 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
0.001645	0.996995	0.000413	0.000310	0.000296	0.000300

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003424_01139.