CAZyme Information: MGYG000004876_00953

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides
• CAZyme ID: MGYG000004876_00953
• CAZy Family: GH38
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
901	MGYG000004876_7|CGC2	102182.08	6.6752

Genome Property

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

• Gene Location: Start: 50660; End: 53365 Strand: -

Full Sequence      

MKILKNIRRWSFLLLVHWLSLPMNAQIAAVEVDKGDEKSTVEDIIIVFKMHFDIGYTDWA
ESILQKYATSMMDETLRSVEATKHLSENEQFVWTLPGWPMKYICENASQENLPKIEDALR
KGRFSVHALPFTWETEASDLESLVRGMSFSSQINRKYGLPLTRGAKLTDVPSHSWVLPTL
LSQAGVKILHIGCNPGSTSPDVPTLFWWEGPDGSRVLTFNWAEYYGSGVMPPVGWKHKTW
LAMIHTHENSEAPDPQTVADVLKEAHEKAPNARVRIGRIEDFYDALMKENPSLPVVRGDM
PDTWIHGFMSMPREMKINKNMQRAIYNAEILNTQLKHWNVTPEFIKPYVDRAVEQSLLFD
EHSFGIALSHGDQGAWKYGDSFTIDRGQGLYDFAEVSWYEKGNRARQAQISIIPSFRKDL
KKMAQNVAMDGRKILVYNTLPWNRSGNVSFHMGVYKKDFQIYGLKDESDGSIVPVYNDYN
HLSFYAKDVPSLGYKTYSLLTEPLADVAQSVRIDEVESVLENRFFKVRINKENGALLSVW
DKQQRKEMVDAKSEYGFGEYIQEKFGQEEMGPYLAKYVKPRSRDWADEEIARPYNPDLKY
KMIRGKLEKISYSKTPNFVRATSFCRMDNGDDYTLTYTLYENSPYMEVCWNICNKKADSQ
PEGGWLAFPFNVSAPSFHLGRTGGIVDPAKDFIKNTNHDYFFLNTGLAVVDKSGKGFGLN
TPDAPAVSLERPGLFRFSGEFVPKKPNVFVNLFNNQWGTNFTEWIEGSFSAKVYLWSVGH
YSHEASLITPVEETRVPLMGVYSEGDGGKLPVSASGVTLSRKGILVTAFGDNIDGEGDVL
RLWEQSGESGKCSVALPGNGYRSGQFCNLRGEPIGTPFPIKGNTFIVDVQAYRPLSILLR
K

Enzyme Prediction     

No EC number prediction in MGYG000004876_00953.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	44	299	5e-16	0.9739776951672863

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	1.40e-47	43	306	1	254	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	3.82e-16	51	306	9	251	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.
cd10814	GH38N_AMII_SpGH38_like	7.50e-13	110	302	63	269	N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38). The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular.
PRK09819	PRK09819	6.79e-11	141	543	98	511	mannosylglycerate hydrolase.
pfam01074	Glyco_hydro_38	8.12e-08	73	304	19	270	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
AOW10778.1	0.0	13	900	6	909
QKJ63408.1	2.47e-299	37	900	26	888
AOW10296.1	4.00e-298	41	900	30	888
AQT68768.1	1.85e-253	41	896	243	1098
AOW10545.1	4.84e-201	31	901	40	921

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.002943	0.995534	0.000804	0.000271	0.000208	0.000195

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004876_00953.