CAZyme Information: MGYG000001735_02215

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides
• CAZyme ID: MGYG000001735_02215
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
898		101682.45	6.5604

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001735	5309957	MAG	Sweden	Europe

• Gene Location: Start: 13097; End: 15793 Strand: -

Full Sequence      

MKRQFIFLVCTFILSVSALKAQIAAIDVDKGADEAAVEDIIIVFKMHFDIGYTDWSESIL
QKYTTSMMDETLRSVKETSKLPKEEQFVWTLPGWPMKYIMENTSETYKSGIEKALQDGRF
RVHALPFTFETESSDLETLVRGMSYSSQINRKYSQPLVRGAKLTDVPSHSWILPTLLTQA
GVKILHIGCNPGSVSPDIPTLFWWEGPDGSRLLTFNWAEYYGSGVLPPATWKYKTWLAMI
HTHENTGAPSPEDVAAVLKEAHEKAPNARIRIGQLEDFYDALMKENPSLPVVRGDMPDTW
IHGYMSMPKEVKINKSMQRIIYNTETLNTLLKQWNITSEPVEPYVEKAIEQSLLFDEHTF
GLAMSHGHQEFWKYGDDFTIARAQGQYDFVETSWYEKGNRAYRAEQYIVPSLRKDLKKLA
QNVDIKGRKVVVYNPLPWKRSGSVAFHMGVYKKNFQVYGLKDESTGKIMPAYNDYNHLSF
YAEEVPSLGYKTYTLIITPLSEDSRTSRIDEAKAVLENKYFKIEINRENGALLSVWDKRQ
QKEMVDKKNEYGFGEYIHEKFGQEEINRYNASYVKPGHHGWADQEMGRPENPDLKYEMIK
GKLIKVKYSQTAHSVSATAFCRTGSGDNYTLTYTLEDNSPYLEICWGIRNKPVESQPEGG
WLAFPFNLSNPSFRLGRTGGVVNPATDFIKNTNHDYFFLNTGLAVLDDQGKGFGLNTPNA
PAVSLDRPGLFRFSGEFIPRRPNVFVNLFNNQWGTNFTEWIEGGLSAKVYLWSVDKYSHE
ASLITPTEETRVPLMATYTENNGGNLPVSSEGIRLSKKGVLVTAFGQDPDGNEGLLLRVW
EQAGESGSLTLYLPAGLKVTKAVPVNLRGEIKGEPVPVRAGKIEFELGAYAPASFILK

Enzyme Prediction     

No EC number prediction in MGYG000001735_02215.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	40	295	5e-16	0.9739776951672863

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	6.46e-43	39	302	1	254	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	1.08e-16	47	302	9	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.
cd10814	GH38N_AMII_SpGH38_like	1.26e-14	111	298	68	269	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.
PRK09819	PRK09819	3.01e-10	137	542	98	514	mannosylglycerate hydrolase.
cd10789	GH38N_AMII_ER_cytosolic	4.76e-07	169	285	125	252	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOW10778.1	0.0	20	898	17	909
AOW10296.1	6.31e-299	32	898	25	888
QKJ63408.1	1.02e-297	30	898	22	888
AQT68768.1	5.74e-263	37	895	243	1099
SDS35267.1	1.32e-223	30	897	27	891

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	1.51e-06	108	335	72	310	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]

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
0.000243	0.999173	0.000148	0.000157	0.000141	0.000129

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001735_02215.