CAZyme Information: MGYG000004088_02265

Basic Information

• Species: Firm-11 sp900548145
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; Firm-11 sp900548145
• CAZyme ID: MGYG000004088_02265
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
857	MGYG000004088_70|CGC1	96857.6	5.6848

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004088	2947168	MAG	United Kingdom	Europe

• Gene Location: Start: 5595; End: 8168 Strand: -

Full Sequence      

MRKERLYYVDGYHGGVRGHMPLGCWRDILETLKTNPDWKLCIDVEPISWEELQARDPAAY
EELRELLKDTSVSARLEMVSGSYGQPYGWITDGESNIRHLTMGLEVMKKHFPWLRVTTYA
TQEPCWTSALPQILRSLHFDYAVLKDPSTAWGGYSNGRDAEVCFWEGPDGSRIPVVPRYA
CEKLAKNWETESVDGTEAFMLKCMEHGIPHPAGMIFQDLGWPSWPRLGGAPGVGEAVVPE
HIVHATWKEYLSSIAEMPVEEPDNIWRVTQEDFLGALPWGERLLVRMARQVRRGERMLLE
CERLHALGSVLSGTVSDQERLKEAWGHLLMTQHHDGWICASTGKDEENWAWKTSAQIYAA
NSLTAPVHRNALQQIGRVVCSDEKDEKEKSGAETACVVNLLGRREERTVSLPITSPHGTQ
SFRVWDGDRLLSSQYMAERRFADGTKNAGTLMFRAALPAFGVKSFRMEPVETEESGCMAW
VDGAFAYLETDVYAIRFDLEHGGTIDSLVDKRRQVELVDRKNERKFNEYSGFFIRENRFL
SNVGQRAEAVVKAEGPVCAELEFQGAVGPVPFTQTVRVLAKESAIRIQAVFHFPEKTYIG
DPHEMTPENDMQDGHRSYHDGRYKLNAWFPTAFEQAHLDKDAAYDVCRSREENTYFSTWN
AIKHNILLNWVDVTDGAQGLAVVADHTTSYTHGKDAPLGLTMAWGWDAGYWWGRRQLKGD
HTLNYALVPHTGDWRKGDVWHECQKLLQEPVVQRMAAASARQCRELIAVEAPVELSAVCL
DDQGRVLARLFNPGPGTPTEITLDAEMFSIAELVELDGTLIGNVPLSVQGDRLTARLELP
SFAIRTLRLTPVPKRQR

Enzyme Prediction     

No EC number prediction in MGYG000004088_02265.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	25	176	9.7e-24	0.5353159851301115

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10786	GH38N_AMII_like	4.06e-10	26	174	31	171	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	6.78e-08	26	176	30	170	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	3.45e-07	25	175	29	171	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.
pfam01074	Glyco_hydro_38	9.79e-07	25	173	29	170	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10793	GH57N_TLGT_like	1.39e-06	15	146	5	143	N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57). 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUR49563.1	1.57e-170	4	850	22	852
QIX66132.1	3.43e-169	4	850	22	852
QKH96606.1	1.85e-168	4	850	22	852
QUT19654.1	7.49e-168	4	850	22	852
BBK89961.1	1.06e-167	4	850	22	852

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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004088_02265.