CAZyme Information: MGYG000000646_00600

Basic Information

• Species: Eubacterium_R sp000436835
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp000436835
• CAZyme ID: MGYG000000646_00600
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1102		125840.63	8.6175

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000646	2069247	MAG	Germany	Europe

• Gene Location: Start: 75421; End: 78729 Strand: +

Full Sequence      

MLTKTAYMVATAHLDTVWRWTIADTVEKFIPDTLSKNFDLIEKYPNYMFNFEGAYRYELI
EEYYPRAFDQIRRYVKTNRWNPAGAEYENGDVNIPSPEAITRNILLGNNYFYEKFKKKSK
DIFLPDCFGFGAQLPQIINDAGLLGFSTQKLSWGSAYPIPFDLGMWVGADGNEIGASFNA
KSYRYKLDGDVRADLSVIDGINKAYVETNMKLPWVNHLYGTGDWGGSPTEESVKNVDESV
RANKDNKLFQVISARSDKVFTKLKRYNNGANGVFIPRYKGDMLMTNHGAGCYTSRTQSKR
LDYQSEQIAHSAEFTCSFASLCGTYDYPKENLNKAWKRSIKHQFHDDITGTSLMEVYNDA
WDDYYSSIAQFKGELTSSLQAISRNMDTSWVPENAVAVSVSNPTQYKRRESVEAKIKLNV
NTPFVKVIDKQKKEVPSQIINKTGKHFEIVFQADVPSFAIHIYAIVPSEEKCQIKTDLKI
SGHTLENSKYRVIFNKNGDLAFLLDKELNKQLITSPIKLAMLHDTGSLAYPSWELRKEDI
DKDAYCYANTPEFEIIENGPARIAIKITREAEYSTINQIVSLYPDSKVIRFDNEIDWRTR
RTLLKAVFPLASSNYVAKYDSGLGYTQRENNSEKLYEVPAQKWADITDKSGNFGVSILTD
CKHGWDKPNDNTLRLTCIHTPVGAFTKETRQDLQDLGRNCFSFGIFGHEGDIENGTNRES
MVFARKLITCEVKKQSEKGEFSQVASLLKLSHDNVVIRAVKISEYDKDALIVRLNNATAV
EQKNAALSVYREFEEVDEVNTSEEFIRKHTPAEKKTIRVSLKPFETMTLKIKFAKAPECK
FNNTYSPMRLNYNVKAFTNYKNMKYNILQGGGYSLPIDLISKNIKVNGIDFYIPHGNSKG
KTPRFDAVACRGQKIRLDGKYNQIYILAGAVSEEDIVATFKIDRKEYKVNFKSMTAPYSK
WDMYGLNQTAHTDDETTFGYEFTHLHHPEGNIVKKARIYLYSLNVKNKKILRFPDNNKLV
IFAMSSAQKEEFTNLAENVIDVVEDNYDFGKIPPIDKITDKTEAITIRAGKIQDQRNGGK
GKGFLRDNIITNIIRSYTKSEW

Enzyme Prediction     

No EC number prediction in MGYG000000646_00600.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	6	268	1.4e-50	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	6.70e-77	7	833	201	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	4.55e-73	5	264	1	250	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.
cd10812	GH38N_AMII_ScAms1_like	3.67e-46	7	246	3	235	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	5.54e-40	5	264	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.
pfam07748	Glyco_hydro_38C	1.26e-38	485	676	1	193	Glycosyl hydrolases family 38 C-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI61027.1	4.35e-217	7	1041	50	1076
BCI61375.1	5.35e-212	7	1030	208	1239
BCI60126.1	2.35e-210	7	1052	43	1096
BCI61374.1	7.61e-206	7	1029	197	1240
BBK86467.1	5.01e-187	6	1029	31	1036

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6LZ1_A	2.90e-61	7	771	284	1013	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	6.90e-61	7	771	284	1013	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	7.80e-52	7	833	305	1096	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
Q9UT61	1.20e-60	7	771	284	1013	Alpha-mannosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ams1 PE=1 SV=1
Q54K67	4.02e-60	7	716	258	969	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q91W89	2.75e-52	5	713	251	915	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	2.76e-52	5	713	251	916	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
P22855	4.10e-51	7	833	292	1083	Alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AMS1 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
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000646_00600.