CAZyme Information: MGYG000001972_00081

Basic Information

• Species: Prevotella sp900315955
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900315955
• CAZyme ID: MGYG000001972_00081
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1347	MGYG000001972_2|CGC2	149308.69	6.3182

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001972	3441323	MAG	Denmark	Europe

• Gene Location: Start: 25761; End: 29804 Strand: +

Full Sequence      

MKQHREIRKMRRWSRQVAMARLGAVAAMLCVAATGAEAQADHKTLFLISDSHLDTQWNWD
VRTTIGEYVHNTMTQNFTLLDKYPYFNFNFEGAIKYRWMKEYWPSDYAKLKKYIASGRWH
VSGCCVDANDVMTTSAESIMRNWLYGSEFFQKEFGVRGGHDVMLPDCFGFSYALPSLARH
CGMTGFHTAKLAWGSSDYGQLPDWGLWQGVDGSQIYAVYKPGAYDTHEDYNHDLTTDASL
LSEINNNYSNYGTAVEIRYVGPRSDHGGGLQDNASSSGENTPYWLNYSASKKTGQIDVRL
ASPDNIFSYLNTYRNQKYRVWNNELPMLTHGVGSYTSRGMLKRWNRRTELLADAAEKASS
LATWLGTEAYPQEAISESWMRMLWQQHHDGITGTSIPRAYTFSENEYVLANKTLANVLTQ
SVGSAARMLDTQVEGTPVIVYNPLSFVRTDIVEASIHVDRRPSPLAVSVFAPDGKEVLAQ
VTGYDEAAQRLKFIFAATVPSLGMAVYDVRIGTPSSLTGSLFQNASTLTLGNGAYSVTLN
KSTGDVQSLMRTRDRRKLVANCSQQMLHDNSTTWPSWEIKYSDVAAQPYATVDDVVSITP
AEVGPLRSSFRVERQKEGSRFVQYVSMNALNNRVDFKNEVDWQTRATMLKAAFNFMFGNP
KATYDISLGTIQRGNRSEGLYEVQGHQWADVSTPAGTYGVSVLNDSKYGWDKPNNSQLRL
TLIHTPGVDNNYTYQSLQDLGVNQFTYSLFPHEGNWGTATQKAASELNQPLTGFVTDKHA
GALGRTVSFVSASTDSVSIKALKKAENSDETIVRVYEWAGKDLKNVSLTFPTDIVSAREV
NGLEEPVGDVAWSGNRLTFDIGHYQPKTFAVRLAAPSAAAPDKVNNTAVGLDYDADVMSY
NDKRTDATGSLVSLAYPAELVPDMVSDGNVTFRMGDRTAGHNNAVRCKGQTVRLSRAAGQ
NKLYVLMMSTRQGGADATFKAGDAAYTFHVPYYTGYVGQLASPFSAGTRYVRDDVAFAAT
HAHNCQNGTDKDYTYLYMYRYVIPLTDDVESVTLPANDDVYLLAATLSDNRADDVQPATA
INTYIDYDELAPDDEKDCGKLLSPVSIKYSAQNGTAEGAALAADMDETTKWCVTPGQDES
PWIEYDFNEPVEVCRWMVLNAGCENTDWISSDFALQAYINGRWQDVDRVSGNTDNYVSRG
VTAFRASRIRLHVIKGQQDDNHTTRIYEFAVYGRNSSTPSGINGISAYSGKGGIRLFGCH
PNPCSGSTTVEFKAPEGLQGAWLEMFDNAGRKVRHQRIPLSGLKTDGGVKSFTCPINQSD
GVYLYRIVADGKGSMPSETKRMIVVSK

Enzyme Prediction     

EC	3.2.1.113	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	45	311	3e-47	0.9256505576208178

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	3.77e-66	45	873	200	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10789	GH38N_AMII_ER_cytosolic	1.02e-65	44	269	1	216	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	5.62e-35	44	311	1	256	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10812	GH38N_AMII_ScAms1_like	1.72e-34	45	269	2	216	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.
pfam07748	Glyco_hydro_38C	3.36e-34	530	732	1	204	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
QUT74823.1	0.0	29	1344	13	1313
AKA50432.1	2.05e-261	46	1232	33	1204
QUU05389.1	2.05e-261	46	1232	33	1204
CAH06062.1	2.89e-261	46	1232	33	1204
QCT76910.1	2.89e-261	46	1232	33	1204

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7DD9_A	7.39e-53	37	882	275	1086	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]
6LZ1_A	7.99e-53	37	902	275	1093	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-]
5JM0_A	1.09e-41	48	847	307	1062	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
2WYH_A	7.22e-12	43	845	26	900	Structureof the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYH_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase [Streptococcus pyogenes M1 GAS],2WYI_A Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS],2WYI_B Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase complexed with swainsonine [Streptococcus pyogenes M1 GAS]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	1.16e-56	45	845	257	1058	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q91W89	1.03e-53	44	876	251	1037	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	3.20e-53	44	877	251	1039	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1
Q9NTJ4	2.28e-52	44	876	252	1038	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
Q9UT61	1.09e-51	37	850	275	1050	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
0.005835	0.991611	0.000782	0.000972	0.000380	0.000374

TMHMM  Annotations     

start	end
17	36