CAZyme Information: MGYG000004172_01326

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae
• CAZyme ID: MGYG000004172_01326
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1281		143235.95	6.2185

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004172	3050906	MAG	United Kingdom	Europe

• Gene Location: Start: 1544; End: 5389 Strand: +

Full Sequence      

MKKLQLLLGGLCLATTLAAGNPGAPDLSKEKTLYLIPYSHLDTQWQWDYPTTIDTYLKRT
LDEGFALLDKYPEYLFNFTGSRRYAMMKEYYPERYERMKKYIAEGRWIVNGSTVDEMDVV
NSGPESYLRHFLYGADFARREFGVEALDFSLPDCFGFPATLPTLVSHAGLKGFTTQKLSW
QAANPIPFNFGIWRGPDGSEIYAGLNCMDYTGKVPENFDIDPEFTDRINRAGKSTGLYAD
MRYYGVGDRGGAPRESDFLNALEASKRHRNFNIRLCGMDQLFRDMEHQKGYSLPTYEGDL
LLVEHSAGTLTSQAYMKRWNRKNERLLQAAERAASLAAMLGTSDYPAERLHKAWDLLLGS
QMHDMIPGSSISKVYEYSHNDEVLVMNLASSVLTNAVGAVSRSLDTKTEGIPVIVYNPVE
RPRQDIAEATVEFAQVPASVRVTSPEGKEVPAQIIGTDGRRTKLIFLADMPASGYAVYSV
TPAEKPAASPLRVTDNTLENDRYKVMIDRNGDVCSVYDKRARRELLREAARWELCYEHPL
RFPSWNMEWADRQLPVKEYVSGPARVLIVENGPVRVAIEVERTLRGNMFRQVISLAAGEP
GNTVRYDNTVKWQMRGRSLRASFPLTVSAPKATYNWESATVQRDNNRSHKFESPSHEWFD
LTDRSGSYGVSVLEDCKNGSDKPNDSTLRLTLLYTPHANREYYGVWQDWGEHAFSYALYG
HEGSWQKAGSDRRGRFFNEPLLTFLPGEKHAGPLGRSVSAASVDKSNVKMLAMKRAEHAD
GYYIVRFNEHYGNTLTDDVQARFCRKIADAYETDGQERRTGPADFTPDGLRFTMGRYGIR
TFAVRFEAPETVPSVRCTPVELPFDTDAVSLNTDRSDGEMAQGSSFAGELFPETLTVDDI
VFRLGDTAPGAHNAVSLRGQRIALPAGDYDRLYLLMSADRDTEGVKIKVDSKSFPIDVQS
WQGYIGQWERRLTDNTLSDVLYGIETGYIKRDPVALLGTHRHTPEGDLSYRYSYIYKYSI
PVSGASTLELPSAPGVKLFAVTAAGGTNDRVVPAMDLYDNFDDREPFELLYPTSYVREGT
EEFGKSCHYLGSKGWTGLNRQKNGTLKDQPARLDATASADDPATKSNRTVRYYCLPFGPE
ASPSGSTQPVECPAMTDGKLGPDRNRTARYYEEGEGRYLLDLGRTVTLKGITTTSFIATK
SGPVRYTLWVSTRSGAKATAADPAAEGWTYVTTVSPRGISPMNAQVSVVEVPQGVKARKV
LLISLGAHSPEAFDEIDLFTE

Enzyme Prediction     

No EC number prediction in MGYG000004172_01326.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	33	295	6.6e-50	0.9591078066914498

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10789	GH38N_AMII_ER_cytosolic	3.71e-74	32	287	1	251	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	4.72e-64	33	846	200	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10813	GH38N_AMII_Man2C1	3.87e-43	32	286	1	250	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.
pfam01074	Glyco_hydro_38	1.91e-41	32	296	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	5.39e-37	33	272	2	232	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDV91863.1	0.0	26	1211	46	1240
AYD48940.1	0.0	26	1069	30	1073
BBL03448.1	0.0	25	1067	29	1073
QEC73841.1	0.0	63	1081	3	1014
AQQ09895.1	7.92e-318	26	1281	27	1277

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	1.41e-59	33	721	283	952	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	3.69e-59	33	721	283	952	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	7.93e-49	33	724	304	959	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
P21139	4.73e-67	14	849	233	1038	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q91W89	4.78e-66	14	849	233	1037	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q9NTJ4	1.16e-64	14	849	234	1038	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q54K67	1.58e-61	33	796	257	1035	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q9UT61	5.81e-59	33	721	283	952	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000345	0.998951	0.000178	0.000188	0.000169	0.000150

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004172_01326.