CAZyme Information: MGYG000003279_02115

Basic Information

• Species: Alistipes sp900541585
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900541585
• CAZyme ID: MGYG000003279_02115
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
544	MGYG000003279_17|CGC6	61348.63	7.6359

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003279	3216844	MAG	United States	North America

• Gene Location: Start: 553604; End: 555238 Strand: -

Full Sequence      

MKIAYRHFLLCILLLSGCLSTAFAKDHVVWRLGEKDGFCREFALHDVAYSDFSKRYTCVT
TICQIGTDDSRKIPCAFPGPKDVWAGKQSGELLVRFGVGRIAPQTRARLVLDFVEVHPYS
PPVLEITVNGFRTKVQTPAGKNSSYFQNRTTDSHDLAVSVALPEGTLQVGENRVSVRNDS
GSWVVWDALTLTADAPVTASKLRDKVELLGAKSSPALMYGEGQELLQPVRMQIANWGAAR
EAEWGYDGRKGGKIRLERGLNQIEAGIPESFSGREVTVAVQAGNKPAGSVSVRLDTVDKW
TIYLVQHTHTDIGYTKPQTEILTEHLRYIDYAVEYCEMTERYPDDSKFRWTCETAWAVKE
WLRIRPEEQVRKFMKYVRNGQIEVTAMFFNMSELSGENAYKAFLAPVGMFKRYGLPVSTA
MQNDVNGVAWCLADYLPDLGVRYLTMGSNNHRALIPFEGPTVYKWESPSGKSLISYRSDH
YNTGNHWGIERGDMGVFSEGVFAYIDKLKRQQYPFDVVSVQYSGYFTDNSPPFRQGVRTD
SRLE

Enzyme Prediction     

No EC number prediction in MGYG000003279_02115.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	301	488	6.5e-16	0.6877323420074349

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	6.77e-83	301	532	1	241	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
pfam01074	Glyco_hydro_38	5.66e-30	301	535	1	226	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	5.06e-11	301	486	1	184	N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
cd10317	RGL4_C	2.55e-04	30	192	1	161	C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
PLN02701	PLN02701	0.002	298	384	38	119	alpha-mannosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL07455.1	3.77e-214	6	535	4	536
BBL02110.1	3.99e-213	5	532	4	532
BBL10048.1	4.47e-212	5	532	4	532
BBL12841.1	4.47e-212	5	532	4	532
QUT72377.1	2.24e-174	9	532	9	528

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000558	0.524637	0.474075	0.000292	0.000229	0.000186

TMHMM  Annotations     

start	end
7	24