CAZyme Information: MGYG000003123_01700

Basic Information

• Species: Chimaeribacter coloradensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Chimaeribacter; Chimaeribacter coloradensis
• CAZyme ID: MGYG000003123_01700
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
894	MGYG000003123_51|CGC1	101056.21	6.6445

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003123	3803778	MAG	United States	North America

• Gene Location: Start: 16255; End: 18939 Strand: +

Full Sequence      

MAKKEVYVVPHSHWDAEWYFTCEDSHILLIENMDYLIALLENDPTFPSYTFDGLASVLDD
YLAVRPENAARLEALITRRRLLAGPWYTQCDTLLIRTESLIRNLLYGTRIAGRLGHSMNI
GYLPDVFGQHAWLPAFFTDLGIQYCVVQRGIYTDQLQGDLNFYWRAPNQKTIATHYLYFG
YGPGKFLSAQPDYLEQRLLPILDQLAAMSQRTPNLLLPAGGDQVLANADFPATVAALNQC
QTAYHFTLADYETYMAETWADTDFPHVIDGELVACQKSRIHRTCHSTRYDIKRQNWETEH
LLLDQLEPLAALASLYGITCPPRLMSRLWKTLFAAHAHNGIEATNADPVNHDIKQRLISV
ERSALSLINLLKKKLSHQVTRQLGRENILMVFNNAPHPLDPLVSAVVFTRSPHFTLRHHG
EPVACTLLRQDAIDGGKKVIVTAQGEKLEPAENYYRSEILFTPFRTPGLGYQAYDLEEQH
PEEHGGAAGSAPAPLVTTQATRIENRHFRVTLQNGTLSLENLRLNQRIDNLLTFVDEGDD
GDEFDFSPLESESPLRFHHFRLIATETGPLISRMTLESVLLLPETIARRTANQRDQPVTL
RTLIQLRHDEPMVRVQHELVNSVTGHRLRVQVNTPVVRPASSYADQGYAILRRETAGRYL
PGWREAGFVEKPVPIHTLENVVYVKDRRCLFGIITRGIKEYEVLPEENSIALTLFRSVGL
LGKDDTLWRPGRASGINNKVVHTPDALMRQKMTFDYALIFEDAGMDEAAVYHAVNRYRGH
HLTYQVQHLNTFEERLERFAIPLPNRPAPAAAMKLAIDNPRVMMSMCKPGPDNALIIRVF
NPTDAPETFTVISDGGHQISRLSLNETPQETLSGAIALAGKAYLTLAIYLHGPH

Enzyme Prediction     

No EC number prediction in MGYG000003123_01700.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	6	263	3.3e-59	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	0.0	1	880	1	862	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	1.79e-134	6	276	2	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	3.66e-61	6	272	2	267	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.
COG0383	AMS1	4.30e-57	1	888	1	939	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10790	GH38N_AMII_1	5.72e-55	6	257	2	251	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
AFK00858.1	0.0	1	894	1	884
AKE93202.1	0.0	1	894	1	884
AXW93167.1	0.0	1	894	1	884
QWR79448.1	0.0	1	894	1	884
AZP34900.1	0.0	1	894	1	884

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WYH_A	2.97e-56	1	722	23	784	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	2.13e-54	1	771	4	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	2.58e-50	3	771	6	793	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
P54746	1.40e-111	2	759	3	745	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	1.93e-47	3	872	2	876	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003123_01700.