CAZyme Information: MGYG000001422_03346

Basic Information

• Species: Bacteroides oleiciplenus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus
• CAZyme ID: MGYG000001422_03346
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
695	MGYG000001422_3|CGC14	78973.71	9.2377

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001422	7071122	Isolate	not provided	Asia

• Gene Location: Start: 752617; End: 754704 Strand: +

Full Sequence      

MKVRVRYLFFLMIGILLGAEVSAKPILKSDSVNPSSIKKIHLIFKTHLDVGFTNFGDSVI
KTYMDDFIPRTLSLTESLRQGGTSERYLWTTGSWLIYEFLKQSDPVMVKRMEKAIKNGDI
TWHALPFSTHTELADPSLYELGIQISKQLDKRFGKNTISAKMTDVPGHTRSVVPILARNG
IKFLHIGVNSASTAPDVPPLFRWQAPDGTSVIVMYQQGYGNQIVLPGTDVMVDIRFTNDN
HGPHSLAQIKSIYKELHEKYPNAEIVTSTLNDVAYETLKIESTLPVITKELGDTWIHGVG
SDPALVSDFRALSRLRLKWINEGKFAFGDEQDLSFGLPLLMVAEHTWGRDVKVYLKDWNI
YLPADFKAARLKSNFKQMEQSWNEKRRYISRAIDNLPLKEKKEAWDILKSLKPSLSSVSG
YSELKDFSKIVKTKYYEIKINPSNGSIIYLKDKKSGQNWANGEHPLFLYSYQTFSNADYE
RFLNQYLIKKVQWALEDFGKPGLEKLNVVSKVWNPTLVSAHCKEDKLGTSVLLKMSVLDD
KRQIVGGSPAEIYVELTFPNDTKEIQATLKWFGKQAYRLPEASWFSFTPIVGKGDWTVDK
MGGIVNFRDVESHGNRKMHSCINGVQLKTIDSATMSVGSLDAPLSMFGNSSLLDFNNKLP
NVEDGVQFCLHNNVWGTNFTMWFDEDMQYRFVVKL

Enzyme Prediction     

No EC number prediction in MGYG000001422_03346.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	3.25e-81	39	297	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.
pfam16477	DUF5054	9.63e-55	299	562	1	285	Domain of unknown function (DUF5054). This family consists of Glycosyl hydrolase family 38 proteins around 700 residues in length and is mainly found in various Clostridium and Rhizobium species. The function of this family is unknown.
cd10786	GH38N_AMII_like	5.77e-20	39	297	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.
cd10814	GH38N_AMII_SpGH38_like	1.14e-06	39	293	1	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.
cd10789	GH38N_AMII_ER_cytosolic	6.91e-04	97	246	52	205	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
QYG92602.1	1.29e-160	37	694	4	689
QYO77724.1	1.21e-132	40	695	6	637
AUS95533.1	6.05e-81	40	691	7	737
AIA19246.1	5.92e-74	37	689	5	711
SDS35267.1	1.72e-69	4	690	4	762

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
0.000283	0.999123	0.000161	0.000140	0.000133	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001422_03346.