CAZyme Information: MGYG000004876_00956

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004876_00956
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
887	MGYG000004876_7|CGC2	101294.49	6.7469

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004876	4781463	MAG	China	Asia

• Gene Location: Start: 57422; End: 60085 Strand: -

Full Sequence      

MKKFLIYLLLLPFVSVMAQVKDGILTCDNETFDLLRDLSKSNLSKGNIMIFTTTHQDLGW
LNHIDACIEDRDTLWLTPYLERLGKDPDFKMDIEQTSIVMEYLHRYPSSKEVFNKYIKEG
RICIGATFVQPYEEMYASESLARQFYYGSRWLKKTFDGYSSSSYFNVDVPGRTLQMPQMM
KKAGIDNLVISRHERGAFYWGAPDGSQVMTYSPGHYIFFYGVLAKNDTAAIKDMAKESVL
WYTKFNDVKKAQTIMPAMLNYELSWDKKPVKNCAILADKWNNLRTIVNAETGKKANVRLP
QFKYAIADEFFRDLRLSTSHIPSHFGERPNVWLYIHGPSHERALTVSREGDVKLPMAEKV
SSFLSLLNGNFISYPTEIMQNAWKDKIYPDHGWNGRNGLYTDNTFLRCYENALAKADLVL
NEQTIRLASMVNTNEKLGYPMVVFNTNSSLRDAVVEVPLRFEGGYAHDLKIVNAKGEEVP
VQCSGVTYYSDNTIEKATVTFVAKNMPAHGLDTYYVTSGEKKIVSQQADNLFENEYYRID
FVSGGIKQIYDKQLNVNLLNTGKFLGGEVITMRSVGNGAGEFDAVQQPDMEGFDKTSNYK
SEWQMIENGPVFAKFKIRTPIRDAVIEQTVTVYNQMKKIDFDVALLNWKMKLYREYRLMF
PLAMKDGKVAYEVPFGKLRVGQDEMPGAAGERYNVENKLQHPRGIGNWLGAYDQKFGVTL
SSSVAVADYIDPTDNAVDYPVLQPILLASRRSCHEAGNEFIQPGDHFYHFSFTSGKTIDE
VFGQSANEPLLSVYRPCKGEKATLNTSYSFVKSDNPNVVITTIKKCEDDESIIVRMYNKG
EDQEKVNLQFCRTPKQIIHTNLIEEEKETVDNIVLGKYAIETFKFKF

Enzyme Prediction     

No EC number prediction in MGYG000004876_00956.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	47	318	5e-40	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.45e-42	50	281	4	253	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.
COG0383	AMS1	8.11e-30	50	887	200	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10786	GH38N_AMII_like	1.86e-26	47	216	1	179	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.
pfam01074	Glyco_hydro_38	1.65e-24	54	315	8	256	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
PRK09819	PRK09819	9.95e-24	80	868	37	852	mannosylglycerate hydrolase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AST52233.1	0.0	1	887	14	906
QUT96672.1	0.0	1	887	1	893
QCX40403.1	2.53e-222	30	883	346	1197
APY11549.1	1.87e-221	30	886	311	1163
EAR02398.1	1.83e-220	30	883	327	1178

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JM0_A	5.07e-11	72	387	313	634	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
Q54K67	3.19e-23	28	885	230	1084	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
P22855	2.77e-10	72	387	300	621	Alpha-mannosidase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=AMS1 PE=1 SV=2
Q9KER1	7.01e-07	50	552	7	547	Putative mannosylglycerate hydrolase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=mngB PE=3 SV=2

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
0.000222	0.999147	0.000147	0.000156	0.000140	0.000133

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004876_00956.