CAZyme Information: MGYG000003214_03175

Basic Information

• Species: NSJ-32 sp014384895
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; NSJ-32; NSJ-32 sp014384895
• CAZyme ID: MGYG000003214_03175
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
782		87304.89	4.616

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003214	5745180	MAG	United States	North America

• Gene Location: Start: 31; End: 2379 Strand: -

Full Sequence      

MNTIFAIGNTHFDPVWLWTWDEAMAGIRSTFASALARMTENPDFTYSFCCPPVFEWIREV
DPAMFESIRARVAEGRWELSEGWYLQPDCNAGLGESYVRHGLYGQNYLLATFGKRAVTVF
NSDSFGHPSSLPQILHKCGIRYYAFSRPDPTEQELPGPLFRWQSSDGSQVLAYRIQEGHA
PDIQTSIQFFSEAIGSSPHDLMLVYGITNHGGAPTKKAIAQLASLSADATLPYHVRFGGT
EDFFSAQTADALPIVTDDLITRNFGVFINNHSVKQHGRQGEYMLLQAERAAWMASSQGKE
YPLAPLTKSWEDILFSQFHDIIGGACIPQAYFHARNLQGRALVTGEEILHKSLQYLTKDM
QMLSSLWNLVVFNLHAAPYSGPIEAEVQWVWELDWYSGALEVFDEAGRTYPCQIIKERSN
IPAFRSRIAFHADLPSLGYKVFGLRQIQGDPTPRPDPTSNSISCGCSSISINPETGAASY
RDERFQLSSLLTPLALSDAGDTWAFNVDGYEAALEDFHFVSSHVLEQGDILSRIQVSYTF
RNSLLELTYSLYANQPYMDCHFRVNWNESQTALKFCLPPCDDPAFLVGLPYGQSSRSFDG
REYPLNEWLTTSHYMVVSESVFAYDTDAENQTVRLSILRSPIAGDLRMGDLDPNQRYDYT
DQGITEGDIRLYMGTWHSGPAAAAAEAMPPIVVDEAFHEGSRGAEESWLRLEGDAALVSA
VKMAEDGSSDLILRLWETRGTDASLTVAPKDCASASITLSPFEIKTLRFSGDTVRETSML
EL

Enzyme Prediction     

No EC number prediction in MGYG000003214_03175.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	3	251	5.4e-55	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	5.53e-81	3	244	1	246	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	9.94e-54	3	259	1	267	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
COG0383	AMS1	3.08e-42	2	771	198	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10813	GH38N_AMII_Man2C1	4.53e-38	3	250	1	252	N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38). The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase.
cd10786	GH38N_AMII_like	6.32e-35	3	172	1	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
QGH33633.1	7.58e-139	3	781	8	812
ALS27092.1	2.81e-137	4	781	6	806
AYB43569.1	4.39e-137	7	781	10	807
QHW33669.1	9.64e-134	7	781	10	811
QIZ10350.1	1.42e-131	3	781	5	805

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JM0_A	5.25e-26	1	356	301	677	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9NTJ4	1.98e-37	2	327	251	585	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q54K67	7.37e-34	4	769	257	1084	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
P22855	2.85e-25	1	356	288	664	Alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AMS1 PE=1 SV=2
P54746	3.46e-12	11	531	14	555	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2

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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003214_03175.