CAZyme Information: MGYG000003887_00083

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1484
• CAZyme ID: MGYG000003887_00083
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
868	MGYG000003887_3|CGC1	98108.81	5.3908

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003887	1242949	MAG	United States	North America

• Gene Location: Start: 5406; End: 8012 Strand: +

Full Sequence      

MNNEKKVCHVIPHSHWDREWYMSFEQHRMRLVELFDALIETMEKHPEYNYYHMDGQYIVI
DDYLEIRPQMRDRLMKLIHDDRIQIGPWYVLQDEYLTSGESNVRNMLYGIKLCKEIGADP
VMTGYFPDAFGNISQAPQILKGFDIDNAAFGRGVGAILEDNKVDPDSPNNPSEIIWRSPD
GSEVIGVMFVRWYHNGMELPTDRDALKKRIDDIVDGLLPSAATPNLLVLNGCDHQPVQTN
LHEVLKVARDIYGDSMEIKQSNFKDYVESIRPYKDSFSLIEGEINGQLTAGAVPLIDTAS
THIPLKIKNHRGQNALDRIAEPLSMIALLSGGKYHDDELFYAWKKLMQNHPHDSICSCSC
DEVAAEMDTRFEKSHEVARFVKDEAMDAVVSKLNTQSLGDRTITVFHTAPGISCGTVKVF
VDFPENSGIDTLHITTAEGTPVPCTVKKLGRTFTYTLPKDRFRQPGYVDRFEVVLISRHE
GIGYETYAVHSGNGKTIERKVKATERGAENESIAFTVNANGSITVTDKISGHVYHNNNIY
EDVGDVGEEYNFRPVQNDVPITTENDTAKVWIEDENDCFVTIGVENTMNLPVGIKDKKRT
SETTAHSITTYFTVTAGVHRIDVTTKFNNQSENHRIRALFVPEIMAERCLAEGQFDVVDR
EITPSPAWKNPCYCQRMQAFFALFEQNRGLMIASRGLNEYEILRDGKNTMALTLLRCVDQ
LGDWGVFPTPSAQCKGEHTLKYSIIPFDKNTKAAAYNEGFTFNGDVFAARSAKPHCGELP
ASSDLFSVSGDYLAFSAFKKAENSNNGILRLYNSDNEPHTLTINFKKPVKAVYETNLGER
RLKEFTIENDKLTTEIGIKKIITLEIEF

Enzyme Prediction     

EC	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	9	272	5.4e-69	0.9256505576208178

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	2.72e-171	5	854	3	863	mannosylglycerate hydrolase.
COG0383	AMS1	8.14e-160	4	868	2	943	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10814	GH38N_AMII_SpGH38_like	1.35e-133	8	287	2	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.
cd10815	GH38N_AMII_EcMngB_like	5.04e-100	6	287	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.
cd10790	GH38N_AMII_1	1.23e-87	9	287	3	272	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
QQA10936.1	2.03e-236	6	866	2	857
AMN35940.1	4.60e-235	6	866	2	857
AWS26233.1	6.51e-235	6	866	2	857
ASY51717.1	6.51e-235	6	866	2	857
SQG39498.1	2.08e-233	6	866	2	857

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	4.09e-174	5	813	6	849	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]
2WYH_A	1.76e-172	6	864	26	918	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]
3LVT_A	3.29e-169	5	813	6	849	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9KER1	3.50e-171	5	867	2	896	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
P54746	9.19e-102	9	839	8	848	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q54K67	1.38e-09	10	836	259	1054	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q54KN4	9.23e-07	9	374	29	414	Alpha-mannosidase F OS=Dictyostelium discoideum OX=44689 GN=manF PE=3 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
1.000083	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003887_00083.