CAZyme Information: MGYG000002330_01384

Basic Information

• Species: Eisenbergiella tayi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella tayi
• CAZyme ID: MGYG000002330_01384
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
687	MGYG000002330_43|CGC2	78137.61	5.7064

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002330	7416064	Isolate	not provided	not provided

• Gene Location: Start: 41113; End: 43176 Strand: -

Full Sequence      

MNTAAKKVIVVFKTHLDIGFTGLAQQVLDKYCLDFIPSAVDLAFRVNTPQYKKFVWTVGS
YLIRYYFAHADAAGCSRLEQAIRLGYVRWHGLACTTHTELMDRRLLDYDLSISHMLDQKF
GIHTIAAKMTDVPGHTMALVPALCDAGIEFLHIGVNDSSRIPSVPGLFRWRAGEQEIVVN
YSASYGESTFLENGTVLEFYHAHDNSAPPSPEELDTLYRDLAQKYPHAHIEAGTMDEFAA
DIRQIRENLPIVESEIGDTWIHGIATDPLKVSQFRRLMLLKEKWITDGLLTPDMPAYHSF
MENLLLICEHTWGMDTKKFLLDFTHWEKSDFTAAREKDSTGYELFSPQNQHIFQALLPEL
EAYKEERGGAGSSYSLFESSHQEQRNYVTHALVALPAREAAEARDFLSFTYPGIPSGAHE
CPVNSPFAAGPYQVTVGAYGELTSLKDMRTGLSRKVSIGLLEYETFGGKEADDCYFAYGR
NLIQNFHWAEPDFGKPGLRYHTQIGHHCYRPFPESVRFWKDTLYVTLLFPEEACAEYGCP
REAMALYRFTEQKIHMELYWKDKDALRSPEALWLEISPGGDNPGCWKMDKTGLLLSPENV
VHNGNRQLHAVQSLSYDAADGRIRIFPLDAPLVSFGGKKLYQPDNCLPDLSLGFSFLLYN
NRWGTNFKQWFDEDMRFSFDILLTCLN

Enzyme Prediction     

No EC number prediction in MGYG000002330_01384.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam16477	DUF5054	2.07e-92	264	555	1	287	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.
cd10791	GH38N_AMII_like_1	1.21e-83	7	262	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	1.28e-04	7	172	1	164	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYG92602.1	3.54e-128	11	679	10	686
QYO77724.1	3.92e-117	11	683	9	637
AUS95533.1	1.24e-58	10	681	9	739
AIA19246.1	6.91e-56	1	681	1	715
SDS35267.1	3.38e-54	10	672	39	756

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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002330_01384.