CAZyme Information: MGYG000003963_01155

Basic Information

• Species: UMGS1696 sp900753285
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900753285
• CAZyme ID: MGYG000003963_01155
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
827	MGYG000003963_11|CGC1	93995.34	5.1164

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003963	2551706	MAG	United Kingdom	Europe

• Gene Location: Start: 56918; End: 59401 Strand: +

Full Sequence      

MKTYMFCNAHLDPVWLWQWESGLSEAISTFRAASEFIDEYPDFIFNHNESLLYEWVEENE
PELFEKIKRQVADGRWNIIGGWFLQPDCNIPSGEAIFRQVLRGRIYFYDKFNKVPVTAVN
FDSFGHAQGLVQMLNKCGYKNYVNIRPGRGNYDFDNEDFLWKGYDGKSEVLVHRSDKGYN
SVFGEVNRELPEWVKRYANSDTALYLWGVGNHGGGPSRIDLDNIAKMKAEGMDIVHSTPD
EYFKTVDRDACPVVDRGLNTLMEGCYTSIIRIKQMHRRLENDLVMVEKMASQAALSGLSK
YEKEKIDDAWRDLLFAEFHDSLPGSCIQPVEDDIIRMLDHGLEIMNQLKAKYFLALCAGQ
EKIKDGNTVPLIVYNPHPFEYTQPIDVEFLLPRQLWHKKFSNPIVYRDGKAVPSQQAKES
GNFYMDWCKRVVFTTPLPPCSVTRLDIHFDVIDSRPAPTTHPEHYKIKIATAHGQVVISC
RTGHIESYVVDGKEFVKPGAFAVNVHTDAYSSWEGKGPLDVYESTGAFHLMTAGEATDFA
GVKGSLIQPVRVVEEGEINTVVEADFIYNNSRMHTKYTIDKLTDEIEIETRVFNAENEMR
FKLFIPTTLKDSEHIGQTIFGREVLKISYADVVSQCWQALADKESALCVIDDGVYGSNAY
DGNLAVTLLRSAGYGAGGSAWGEPFREPMYQQRMDQGERRYRFRVMAGKRDDILLRADRE
AAQFNQKAYALAFCPSGNGTKPKELISVDRENVTLSCFKQSERDAAKYIFRLFEAQGTEC
DAHIELPIAGVSLDTHFTPFEIKTFMLADGKVTETDMLEGAVPLSNE

Enzyme Prediction     

No EC number prediction in MGYG000003963_01155.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	3	249	1.9e-56	0.9330855018587361

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	4.33e-93	4	246	3	249	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.
COG0383	AMS1	6.41e-54	8	805	205	939	Alpha-mannosidase [Carbohydrate transport and metabolism].
pfam01074	Glyco_hydro_38	1.61e-52	9	253	8	262	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	1.40e-37	8	249	7	258	N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. 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 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1.
cd10813	GH38N_AMII_Man2C1	1.10e-36	8	249	7	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGQ94579.1	9.63e-245	1	819	1	824
BBH19161.1	1.37e-241	1	819	1	824
BBH22115.1	6.89e-240	1	819	1	824
BBI35196.1	8.84e-237	2	819	3	822
QTH40091.1	8.05e-235	2	807	3	808

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	1.09e-40	2	822	282	1085	Structureof S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_B Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_C Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-],6LZ1_D Structure of S.pombe alpha-mannosidase Ams1 [Schizosaccharomyces pombe 972h-]
7DD9_A	4.53e-40	2	343	282	639	ChainA, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_C Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_E Chain E, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct],7DD9_G Chain G, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein [synthetic construct]
5JM0_A	1.67e-30	2	330	303	650	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	6.07e-45	8	788	258	994	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q91W89	2.48e-43	8	793	257	998	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q54K67	2.60e-42	2	805	256	1082	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
P21139	5.27e-40	8	793	257	999	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9UT61	1.72e-39	2	343	282	639	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1

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
1.000054	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003963_01155.