CAZyme Information: MGYG000002325_00441

Basic Information

• Species: Listeria monocytogenes_B
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Listeriaceae; Listeria; Listeria monocytogenes_B
• CAZyme ID: MGYG000002325_00441
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
860	MGYG000002325_1|CGC12	97441.51	4.8085

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002325	3017944	Isolate	Canada	North America

• Gene Location: Start: 455934; End: 458516 Strand: +

Full Sequence      

MVKAHIVNHTHWDREWYFTSADALVLSEQLFTEVIDELKKHPEANFVLDGQLSILDDYVA
LYPEKLADIKQLIADKQLFIGPWFTQTDAFFAHGESILRNAMIGIFDSKKYGDYMEIGYL
PDTFGFNAQMPTLLEHAGFDNVIFWRGIHLGEHVASPYFKWQGLGEEASIYAINMPQGYG
TGMLLEPTSAYVDGRLDPAIDFIEKYSKTTEVLIPSGNDQLNIISNFAEKLVKINKMGRH
DYQLSTYQDFIQYVRELPDLEEYRGEFRSPVLARVHKTIGSSRMNIKLKSASLEQKLLTR
IEPLLVIAKASGISISERLLMHTWKKLLEGQAHDSLAGCVSDPVAEDILHRMKEADELCD
SIENTIVKKIADDLSLAANEIIVFNTDLHDFDGYKEIQVVTEHKNIHFPAFPDATIVQEE
FIPSRENVLEETPAGNRFIEEPGYYVLQVRVKVELPGLGYRVIAFEENDRELDSMIASND
VAITNDFYKITFENGEIALEKPNGERITSFITLEDDVNAGDTYDYSPLAGDIAELFTFSE
VKTEKSSEVERLILTGKSDFPLDRLTKEGHGDLQIKLILEVKKGSELLDVKVEVDNQIKN
HRLRLKVNTGVKTDYNIASLPFGYIKRKPVVPANWRETYSEMPIDIEPLEQSVTLTNEAE
SCTIFTQGIKEYQQLDQYLALTLLATTGQLGKPDLAYRPGRASGDTTKKGHVLIETEGAQ
LLGKHEFSLAIYLGDQAFDEHKTAERTKAFNQANVSYQRQPFNHFLHRLDNKIQKTERKL
GAKQTLGMLNLPKEYLVSACHPSYYSADKYIIRLENPTNTPQKLALSDMSFEYVNAIEEV
VANDNNTIPAYGAVTLRLEI

Enzyme Prediction     

No EC number prediction in MGYG000002325_00441.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	3	257	3.7e-65	0.9368029739776952

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0383	AMS1	0.0	1	859	3	942	Alpha-mannosidase [Carbohydrate transport and metabolism].
PRK09819	PRK09819	4.51e-169	3	817	5	822	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	9.86e-140	3	271	1	270	N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38). The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity.
cd10814	GH38N_AMII_SpGH38_like	5.38e-60	3	270	1	270	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.
cd10790	GH38N_AMII_1	1.99e-57	3	220	1	217	N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38). This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. 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. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that 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. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOF65005.1	0.0	1	860	1	860
AKG87418.1	0.0	1	860	1	860
APO63498.1	0.0	1	860	1	860
AMD26380.1	0.0	1	860	1	860
AGR05058.1	0.0	1	860	1	860

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WYH_A	1.30e-58	3	728	27	803	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]
5KBP_A	6.40e-55	3	732	8	793	Thecrystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583],5KBP_B The crystal structure of an alpha-mannosidase from Enterococcus faecalis V583 [Enterococcus faecalis V583]
3LVT_A	7.84e-52	3	732	8	793	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
5JM0_A	1.71e-07	7	360	307	671	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
6LZ1_A	1.72e-07	7	143	286	423	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-]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54746	3.93e-103	3	704	6	724	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	2.81e-45	4	691	5	754	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
Q91W89	9.01e-09	5	350	253	593	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q54K67	9.13e-09	7	497	260	751	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
P21139	1.18e-08	5	350	253	593	Alpha-mannosidase 2C1 OS=Rattus norvegicus OX=10116 GN=Man2c1 PE=1 SV=1

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
1.000065	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002325_00441.