CAZyme Information: MGYG000002437_02974

Basic Information

• Species: Blautia hominis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia hominis
• CAZyme ID: MGYG000002437_02974
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
815	MGYG000002437_4|CGC2	93866.07	5.1264

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002437	5878941	Isolate	South Korea	Asia

• Gene Location: Start: 155744; End: 158191 Strand: +

Full Sequence      

MMKKIILVFKTHFDIGFTDLAENVIEQYGGSMLRQVLETCRATEDMGKLKYVWTMPSWPL
WTVTKKCSDEMRPELEHYIENGQIAWHALPFTSHTDFCGEEEYLEGLRFGKELSEKYGKP
YPIAAKMTDVPGHGLMLPEILGATGIHFLHLGCNAFATPPKVPELFFWKAPSGRKVLTMY
CKGGYGSSLEAPEEWEYPVWMSLVHTHDNCGPHSAEFIKKLAAEAHDLYPEAEIVCGTMD
DFCRELENYDLSGVPVVEQDLADTWIHGIGAYPREVREIRECRHRAARLQKLAGQTIRDE
ENGKKAEMILKEYYESMNLFGEHTWGADVKTWLGPDRVYKKEEFKKARQEKNYQFMEQSW
EEQRKRAETCKNLLERYEQDLEKDREKREWLYNPLTEPYTGWVQGDSEPVYVKGLAPLAC
TKLERSMGDKAPKNSDDLTVEDHPEGSSVENHRYRLEFSAADGTITAVYDKKLNRRLLEA
QKDTGIFSYQYTRHGIEKITEFLRSYGYRFSTWGIQDYGRENYPECKDETYKPCFVKTEV
NGRTISFFYKGETSARLYGDCHQAEVRITLPDEGEELFVSLLLSGKEASPYVESGSFCLP
LAGDLDNYRINKPGSVLNPKTDIADNGNHVLYSIEEFAAADNRRSGVCVMPLDTPLMSIG
EDGIYTYRHQYEEHTPILYFNTFNNMWGTNFPQWQEGDSEYRFVLWGYDAKDADGLLERS
VQLGEGIQRTSCEAKKLNLTLPCHMQLLNIKQGEDGMILVTRDLRGEEAEGTVCMPGYYI
TEIDYYGRQTGELKRDSLTFVKKKYGLHIFKVEKV

Enzyme Prediction     

No EC number prediction in MGYG000002437_02974.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	4.71e-61	4	267	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	5.84e-15	4	230	1	225	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.
pfam16477	DUF5054	1.53e-11	322	577	46	269	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.
cd10814	GH38N_AMII_SpGH38_like	3.52e-09	70	263	63	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.
cd10790	GH38N_AMII_1	3.20e-06	70	193	62	184	N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. 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. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that 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. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUS95533.1	5.59e-162	5	773	7	811
AIA19246.1	3.67e-129	2	705	5	715
AOW10778.1	7.14e-100	5	717	37	786
AQT68768.1	2.62e-95	2	792	243	1078
SDS35267.1	1.92e-88	7	720	39	782

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000078	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002437_02974.