CAZyme Information: MGYG000003701_02851

Basic Information

• Species: Parabacteroides sp003480915
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp003480915
• CAZyme ID: MGYG000003701_02851
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
866	MGYG000003701_6|CGC9	98848.2	6.2953

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003701	6084075	Isolate	China	Asia

• Gene Location: Start: 227443; End: 230043 Strand: +

Full Sequence      

MKYSLLIAFCVVSFCTTAQSNYLKEGHVNFALSSHQDMAWMDVPDKCTEFRIEKLLMPSL
RMLEKDSSYCFTMEYALTLEEFLNKYPERKDELMQLTAKKRLDWGATFNQPYEGMLSGES
LIRETYLGKRWLQKQFPGCEFVTAFNPDVPGRSLQTSQIHAKAGIKYGIISRFEPGIYQW
FSPDGSSILCKSNGIYCDYARTLAGKKEKEEKKEYIRSIVHFWDPYYKENKMPSELFFLH
TDDNEEPYDYQQIFKELSAEKDMPEFGYTTISTAMDKLVSKKSKPTRLEGEWPDLWLYIH
NPTHHEAVSMMRDAQRNLVNVEKFGAVRGLLTGSFASYPQDKLNEAWKCAIYPDHGWGGN
GGYITDEIYKEKFRQSQASANEMLEDVLGEIGGMIEHKQEGLPIVVFNPESWLRNDIVIT
KVNVYGLGRGHFVLTDDKGQHIPFQYLPIKGQTKDGDIQIAFQADSIPSIGYRSYYLKHV
KDEIFEDAVTASNKIDIDNPYYRISFAAGGIKSIFDKRLNRELLRTDKFLGGEVFCTRSV
GNGAGEFKEIQPITMEGFEKSSDYSPSWSIIESGRVREVRECRSKFKHATVIQRIIAYQN
FPKIDIEIDLEGFTGEAYQEFRMTMPLNQSSSLISYEVPMGVVEIGKNDLSISAGHAGGL
HYTTPLNETPLRECQNWFASSDDLSNVMLSSSVGVFGYKDATSNPVDYPVLQPVLLASRK
SCHWKGNWYLQQGNHSYRFSLHSSDGDWKKTHQLGTQSAQPLLTAVGVKNGNNKILSPLQ
SFFSVDKKNVMVSTIKKCEDDDNVVVRLFDIEGMDSDVSLWSFKPIKKSCQTNIIEEPQK
LIDNKGDILPVKIGHHSIETYKLEYK

Enzyme Prediction     

No EC number prediction in MGYG000003701_02851.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	33	283	7.1e-34	0.9219330855018587

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	6.03e-24	27	189	1	176	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ 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.
cd10786	GH38N_AMII_like	2.29e-21	33	189	7	171	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.
COG0383	AMS1	5.22e-21	115	865	285	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
PRK09819	PRK09819	1.22e-16	60	638	37	606	mannosylglycerate hydrolase.
pfam01074	Glyco_hydro_38	2.97e-16	34	190	8	172	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AQT68758.1	4.32e-241	22	863	263	1112
AQT68763.1	4.50e-227	26	862	277	1118
AQT68754.1	1.23e-201	22	863	283	1126
APY12816.1	4.96e-186	22	866	112	950
AST52226.1	5.99e-177	22	863	116	951

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q54K67	1.75e-11	35	862	264	1083	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG 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
0.000215	0.999190	0.000142	0.000154	0.000136	0.000132

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003701_02851.