CAZyme Information: MGYG000001735_01860

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides
• CAZyme ID: MGYG000001735_01860
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		37765.57	5.8386

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001735	5309957	MAG	Sweden	Europe

• Gene Location: Start: 42961; End: 43968 Strand: +

Full Sequence      

MKTIAGNLFVWCVIILCVFSGCDQKKATPDPVRAKEVADLRFGMFICWSYSTFSGKEWTG
EPHDVSFFRATSCNTDQWARTAKEAGMNYILFLTKHHDGFCLWDTQTTDLKVTNAPLKTD
VLKQLRASCDKYGIKLALYFSEGDWNWEGAERGRSQKGGSNPDMKKAQLKELLTQYGPVE
FIWFDHAVGDGGLSHEETTAWVHQFQPDCFAGYNHGAPSGRLSLRERGCAGPLGGDNLTW
VEDAGKNEKAYDGYLVAEFTYPLLPPHEGGADWFYSLPQHDSLAFPAEKIYKDYKEAVEY
GNIFSLNIGPDYNGNIRDIDCKVLREVGRMIKENK

Enzyme Prediction     

No EC number prediction in MGYG000001735_01860.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	38	334	7.1e-59	0.8497109826589595

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01120	Alpha_L_fucos	3.41e-39	26	334	7	331	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	2.81e-37	39	334	25	333	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	1.08e-25	39	334	20	315	Alpha-L-fucosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGY43460.1	5.17e-152	11	335	24	355
AQT67234.1	3.70e-113	25	332	387	701
AFD06713.1	4.93e-43	18	333	17	351
QNA45994.1	1.78e-41	1	331	3	345
QEC55523.1	2.51e-41	8	331	11	345

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZRX_A	3.78e-36	45	326	47	347	Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
5K9H_A	1.14e-28	19	320	27	341	Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
6GN6_A	3.75e-28	41	334	38	347	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]
3UES_A	2.96e-26	33	333	28	349	Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3UET_A	6.65e-25	33	333	28	349	Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8GW72	2.25e-29	44	330	52	339	Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3	2.87e-23	28	326	30	336	Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713	2.65e-13	39	331	36	342	Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q99KR8	6.34e-12	41	334	48	357	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q9BTY2	2.75e-11	41	334	54	363	Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000153	0.999922	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001735_01860.