CAZyme Information: MGYG000003525_01299

Basic Information

• Species: RC9 sp004556005
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp004556005
• CAZyme ID: MGYG000003525_01299
• CAZy Family: GH29
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
463	MGYG000003525_28|CGC2	53532.63	4.9721

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003525	2213098	MAG	Fiji	Oceania

• Gene Location: Start: 57471; End: 58862 Strand: -

Full Sequence      

MNIKKLFISAALMLAAFASVANAQEEKKYIEPLEEGVKQRIRDWQDQKFGLFIHWGTYSV
TGVIESWSLDPRHIEWCYKFRPKDMSYEEYVRSYENLITQFNPVSFDPETWAKAAKYAGM
KYMVFTTKHHDGFSMFDTQQNDYKITSDRCPFHTSPKANIAKELFDAFRAEGIMPGAYFS
IADWYNDDYWWDYFPPKDASPNYPIDRFPEKWNRYLDFLNAQVDELTGGEYGDLQMLWFD
LATTIPLDNYDRIAATARKNQSDIMIVARSTGTIYENYLTPEQKIPDTALPYPWESCITM
THAWSYRPGAQYKPTRTILEMLVQIVSRGGNLLLNVGPRPDGTLEDTAYERLREIGDWMQ
VNSEGIYGTKPYTICQDGKVCFTTKDGYVYAFYIADEDETEMPSEITFNGVVPAGQKNSV
TLLGYDRPLVWSGNGEGGLRVVIPEKVRKNKPCEHIWCLKIKL

Enzyme Prediction     

No EC number prediction in MGYG000003525_01299.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH29	14	368	7.2e-103	0.9566473988439307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01120	Alpha_L_fucos	4.05e-113	24	364	1	333	Alpha-L-fucosidase.
smart00812	Alpha_L_fucos	7.82e-98	23	393	1	370	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	3.14e-42	54	378	1	331	Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam16757	Fucosidase_C	2.31e-07	378	462	7	90	Alpha-L-fucosidase C-terminal domain. The C-terminal domain of Structure 1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT88497.1	1.65e-186	22	463	30	469
ALJ60491.1	2.35e-186	22	463	30	469
QEH40709.1	2.14e-152	5	462	2	471
QJD77328.1	3.47e-152	8	461	10	474
QJB41770.1	4.54e-151	4	449	2	462

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6GN6_A	2.92e-69	38	391	28	376	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]
7DB5_A	6.47e-37	38	370	31	363	ChainA, Alpha-L-fucosidase [Vibrio sp. EJY3]
1HL8_A	1.49e-35	41	394	20	388	CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL8_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL9_A Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8],1HL9_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8]
4JL2_A	1.51e-35	35	367	11	348	Crystalstructure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482],4JL2_B Crystal structure of a bacterial fucosidase with a monovalent iminocyclitol inhibitor [Bacteroides thetaiotaomicron VPI-5482]
1ODU_A	2.05e-35	41	394	20	388	CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8],1ODU_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q99KR8	3.90e-45	31	459	29	455	Plasma alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca2 PE=1 SV=1
Q5RFI5	4.10e-43	31	461	33	461	Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1
P04066	2.95e-42	12	461	20	462	Tissue alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA1 PE=1 SV=4
Q9BTY2	3.00e-42	31	461	35	463	Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
P17164	5.13e-41	12	461	16	458	Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 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
0.000294	0.998918	0.000240	0.000174	0.000173	0.000157

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003525_01299.