CAZyme Information: MGYG000004006_01769

Basic Information

• Species: Alistipes sp000434235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp000434235
• CAZyme ID: MGYG000004006_01769
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
954	MGYG000004006_7|CGC3	106496.34	5.2995

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004006	2755781	MAG	United Kingdom	Europe

• Gene Location: Start: 103558; End: 106422 Strand: -

Full Sequence      

MNKTLLAIALFGLAAGETSAQQIGRVARVEPVRYEKRDGRLKILSYVKLSEAPARKTVLQ
LGDEPLAVEAGSTGDSLLVWLPMIGKSDVLTLRSGRKVLSSKAVEAPIPDDWGYFRNGTI
HIIQSSHQDIAWMDTPEYCRTERIEDIIIPALDIMREDPNFTFEMEQTLNLMEFLEAHPE
RRDEVIERYKEGRFVWGATYNQPYEGLASGEQLVRQAYYGRKWIRENLPGCDDRTANNVD
VPGRTMQMPQILAKSGIRNLFVSRMREGLYDWYSPDGSSVLTYTPGNYGWATLMWKFFEK
DAVTAFERLHPRSRLWSDYFRSRHIPPHYAVLMSCDATKPVNFAPVIDEWNRIAELAEVE
LPRLKCSTAEEYLALVDTPEAQMEEVVGERPDLWLYIHGPAHYQQTVAKREAGVLLPAAE
LFTAVNNVCLDGSWDYPRAAFDRAWMASIYPDHGLGGKNGEITDRIFGDSLSVARDLGRS
LLDASLRKIADRVPEQAGNWVVFNDLQWDRTEVAYLPAGDRPAVVCTSDGRELPVQRIER
DGRECLAFVAEGVPSFGYAAYRVKPVAKEPRPVVPAGVEQGDNYYRNAFYDIVLGDGGIV
SLYDFEQGCNLAETSRFAFGDILDAGYKGNGAGEFNRIADLEVDDQTLVSAQPASWRIVA
TGAVCTTFENAVQTAFARVIQRITVYHAIKKIDFDVTLENFTGEHNRQYRILFPLNMKTA
SSRIHYEVPMGVAEVGVSEMKSVPGGWSWGGTYVHHPADSHPREIQNFISASGNGFGVTM
SSCVAVADWIDPSRDQSDYPVLQGILLSSHKSCHGEGNWYHQTGTHSFRFSILGHEAGWQ
NGYCFGVGANHPLLPVAREGRGGDLEASCSFIRISDPLVSLTTLKKADGGNALILRLTEM
EGVDKTVEVTLPFDVKRVTRTDLIEEGGEPVAGSGRRLTLRLGHHAIETYKLEL

Enzyme Prediction     

No EC number prediction in MGYG000004006_01769.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	119	378	1.9e-42	0.9330855018587361

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	3.47e-51	119	351	1	253	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.
cd10786	GH38N_AMII_like	2.21e-31	119	352	1	251	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.
pfam01074	Glyco_hydro_38	3.11e-31	119	374	1	253	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10789	GH38N_AMII_ER_cytosolic	4.83e-25	119	295	1	184	N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. 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.
cd10814	GH38N_AMII_SpGH38_like	1.58e-22	119	389	1	266	N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT96681.1	0.0	1	954	1	953
AST52226.1	0.0	1	954	1	953
APY12816.1	6.94e-293	3	953	2	948
AQT68758.1	1.09e-230	33	952	183	1112
AQT68763.1	2.33e-228	97	951	258	1118

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	1.23e-15	120	926	9	875	Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
3LVT_A	2.92e-13	120	926	9	875	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54746	1.69e-15	120	721	7	629	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB 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
0.000368	0.998932	0.000213	0.000163	0.000158	0.000137

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004006_01769.