CAZyme Information: MGYG000003638_01411

Basic Information

• Species: Prevotellamassilia sp004557035
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotellamassilia; Prevotellamassilia sp004557035
• CAZyme ID: MGYG000003638_01411
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
502		55189.29	5.3049

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003638	2109164	MAG	Fiji	Oceania

• Gene Location: Start: 1251; End: 2759 Strand: +

Full Sequence      

MNKTTKFLLPALLAAVPFTSWAQSEFTLSTATPANAEGEPAPVFPVPSDRQLKWNETEFY
AFFHYGMNTYTGQEWGYGNERESQFAPTAAPNPRQWLEAAKAAGMKGGIAVVKHHDGFCL
WPTETTTHCVKLAGNDFGKNTNIPRDFANAARDLGMKYGFYVSPWDRNSLYWGDGTDNYA
KKVFLPQCAELATYGHDQFEMWFDGATGGGGYYGGSSNTNRSISSAELYYDIPNLRDSIH
NVCPDCVMWGVGGEARWIGNEAGWAGETCWSMGNGTSGDENGYEWHPGESDAKGTENGWF
WHSGETVKSAERLFQMYLETVGRNATLILNLPPDQSGSLPAATVNRMTELGNLISTRLGT
DLAPSATVTVSDARPNGATRTYVAANITDDNKDTYWAASDGQKTATITFTWPETKTVRYV
SMMEYIKLGQRVKGFNIEVSTDGTNWTAVGGNIAKTTIGYKRIIPLNGNTSNSYGDGYQA
KYLRINITDAKSCPTLHTVQIF

Enzyme Prediction     

No EC number prediction in MGYG000003638_01411.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	48	354	1.6e-58	0.861271676300578

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3669	AfuC	4.78e-44	40	442	4	386	Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120	Alpha_L_fucos	2.04e-27	65	352	60	326	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	6.24e-23	64	352	50	328	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.
pfam00754	F5_F8_type_C	4.45e-11	379	489	9	114	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ13684.1	7.11e-220	35	502	34	500
BBA29772.1	1.84e-212	2	502	3	508
QFQ12303.1	4.22e-212	33	502	30	492
QUB69927.1	1.50e-211	2	502	3	508
QFQ12382.1	1.71e-211	33	502	30	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K9H_A	3.10e-68	42	464	34	434	Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
3EYP_A	1.70e-65	41	502	4	454	Crystalstructure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],3EYP_B Crystal structure of putative alpha-L-fucosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron],4OUE_A Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OUE_B Crystal structure of an a-L-Fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with IPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_A Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482],4OZO_B Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG [Bacteroides thetaiotaomicron VPI-5482]
6TR3_A	4.61e-61	35	471	17	480	Ruminococcusgnavus GH29 fucosidase E1_10125 in complex with fucose [[Ruminococcus] gnavus E1]
3UES_A	3.67e-60	47	464	19	447	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]
6TR4_A	6.55e-60	35	471	17	480	Ruminococcusgnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1],6TR4_B Ruminococcus gnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7XUR3	2.61e-66	40	502	33	476	Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q8GW72	2.13e-65	40	464	31	447	Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
P49713	2.41e-09	92	355	98	343	Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2
Q99KR8	7.11e-09	92	351	107	351	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q9BTY2	3.67e-07	92	352	113	358	Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2

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
0.000639	0.998466	0.000274	0.000224	0.000197	0.000179

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003638_01411.