CAZyme Information: MGYG000003941_00192

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes
• CAZyme ID: MGYG000003941_00192
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
873	MGYG000003941_3|CGC3	97888.6	6.8915

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003941	2202352	MAG	United Kingdom	Europe

• Gene Location: Start: 53387; End: 56008 Strand: -

Full Sequence      

MKPICSGASLLRVRPCQTPNGKPTRLSIPAVGRKMLLGALLLLGNPLAAQRPAYFADGYH
GGIYGHYPVRWKTRFICDQLEAHPEWRIGLEIEPETWDTVAVRTPRDYARFKRLATDPRV
EFTNPTYAQPYCYNISGESLIRQFDYGMRKIRSHFPDVKFTTYAVEEPCFTSSLPQILRL
FGFRYASLKCPNTCWGGYMAPFGGETVNWIAPDGSSIRTVPRYACEALERGSVWQTTAWG
NSTEYLEACARQGIARPIGMCYQDAGWRNGPWIGSGDSIRNHSTYVTWREYFERIAPDSQ
PEDYRMSQEDVRVSLMWGSQVLQRIAREVRHAENSIVGAEKLCALATLASGAGCDRAAID
EAWRTLMLAQHHDSWIVPYNGLHGRGTWADHIRRWTAATDSISDGLAAGAMRSIAPARER
GRWRVRLVNTLGEARREVVAVALPEEFPCEGIIVKDARGRKVESTLLRTAEGARELLFEA
EVPPFGYTTYTLAEGHAKECTATAAATAEPLVVENDLYRLRIDPARGGVITSLVARRLGN
REIVDAASSYALGELRGYFYDERRFRSSTESPAEVVLLCDNDLVKRIRIRGTIASTPFTQ
TITLRRGDPKIDFDLAIDWRHNVGIGAYRERNAFGRNRRACYDGRYKLNVWFPTTLVAPR
LWKDAPFDVCESRLEDTYFSTWDNIKHDILLHWVDLAETDGAGVALLTDHTTSYTWGIDA
PLGLTVQYSGAGLWGRDYPIDGPTHLRFALIAHDGHWDEGGVQEENTRWNEPLYAAVGRT
FTDGEASWLDLAGSGYELSAAYPENGAIIVRLYNASGDETPHTLRFGDLFSKIEAVDLRG
EPLETPAIQTRGGGTEVELSMPRFGLKTLRLTK

Enzyme Prediction     

No EC number prediction in MGYG000003941_00192.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	75	220	5.7e-29	0.5278810408921933

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	2.24e-18	135	873	286	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam07748	Glyco_hydro_38C	5.04e-14	513	711	1	180	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10789	GH38N_AMII_ER_cytosolic	1.21e-10	105	217	60	169	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	1.32e-10	105	230	60	190	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	7.23e-09	61	219	19	172	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
BBL06663.1	0.0	1	873	1	880
BBL11622.1	0.0	39	873	43	883
BBL08830.1	0.0	39	873	43	883
BBL00893.1	0.0	4	873	11	882
QNL41054.1	0.0	35	871	6	852

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
0.451457	0.529250	0.018326	0.000449	0.000283	0.000233

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003941_00192.