CAZyme Information: MGYG000000284_01479

Basic Information

• Species: Parabacteroides sp900540715
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp900540715
• CAZyme ID: MGYG000000284_01479
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
335		37781.59	5.6117

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000284	5935659	MAG	Sweden	Europe

• Gene Location: Start: 35847; End: 36854 Strand: +

Full Sequence      

MKTIVGSLCVWYTIILCVFTGCNQKKVIPDPVRAQEVADLRFGMFICWSYSTFSGKEWTG
EPHDVSFFRATSCNTDQWAKTAKEAGMNYILFLTKHHDGFCLWDTQTTDLKVTNAPLNTD
VLKKLRASCDKYSIKLALYFSEGDWNWEGAERGQSQKGGSDPEMKKAQLKELLTQYGPIE
FIWFDHAVGDGGLSHDETTAWVHQFQPNCFVGYNHGAPSGRLSLRERGCAGPLGGDNLTW
VADAGKNEKAYDGYLVAEFTYPLLPAHEGGADWFYSLPQHDSLAYPAEKVYKDYKEAVEY
GNIFSLNIGPDYNGNIREIDRKVLQEVGRMIKENI

Enzyme Prediction     

No EC number prediction in MGYG000000284_01479.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	37	334	2.3e-58	0.8526011560693642

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01120	Alpha_L_fucos	9.92e-39	39	334	24	331	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	1.06e-36	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	1.03e-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	2.43e-150	11	333	24	353
AQT67234.1	1.87e-113	33	335	395	704
SDT40017.1	7.40e-40	14	334	9	323
QNK62939.1	1.24e-39	29	334	24	347
QOD59462.1	1.57e-39	12	333	8	347

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZRX_A	4.76e-35	26	326	29	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	8.38e-29	19	329	27	357	Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
6GN6_A	5.15e-28	33	334	30	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	3.68e-23	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]
4PCS_A	3.87e-23	21	329	7	338	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8GW72	6.92e-31	27	330	34	339	Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3	2.87e-23	27	326	36	336	Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
P49713	1.97e-13	68	331	92	342	Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q99KR8	8.49e-12	41	334	48	357	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q6AYS4	4.85e-11	41	334	46	355	Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1

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	0.000005	1.000047	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000284_01479.