CAZyme Information: MGYG000001635_00106

Basic Information

• Species: Longibaculum sp900538465
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum sp900538465
• CAZyme ID: MGYG000001635_00106
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
854	MGYG000001635_1|CGC4	99905.18	5.5211

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001635	2765607	MAG	China	Asia

• Gene Location: Start: 122109; End: 124673 Strand: +

Full Sequence      

MAKQVHIVPHMHWDREWYFSAEESKILLINNMEEIMERLEHDPDYPTYTLDGQTSVLEDY
LTMMPQNKERLKKLIQDGRLIIGPWYTQTDEMVVGGESIVRNLLYGHKDCQEFGNCMNIG
YLPDSFGQSGQMPMILNGFDIHRSMFWRGTSERMGTDKTEFYWQSDDGSRVLTQLLPLGY
AIGKYLPTDFDELKKRCDKYMPVLDKGATTDHILIPNGHDQMPLQKNITDVMEQLHHIYP
DKHFFLSSYDNLFKELEKKDNYDTLHGELLDGKYMRVHRSIFSSRSDIKTMNTMIENKLT
NILEPLASLAYTLGFDYYHGVIESIWKEMMKNHAHDSMGCCCSDKVHQEIVNRFMIANEK
IDRLIDFYKRKITDAMDCHISLDKLTVFNLLTYQRKEVIEAQITTRMKSFKLVDKDKQII
PFEIVHQEIIDPGIIDRQIVHYGNYDPFVRYTIHFKDSIPAMGYKTYFILEDEIQKEISM
QDCSLFENEFYKINFHDNGTIDIYDKKRDCLYQEVLLLEDGSDDGDGYDYSPIKDDYIIR
SHHVKANIEIQQKGMKKVAQISYDMSLPKDLNSRKEKVCDGQIHVCFEIELKDGSSYIGI
KAHIQNNVKDHRLRVMIPLQIQGKMSISDFQFGMIKRPVYDLAMDVWEKEKWSERPDSIY
PMLSYVTIEGSHMAAITNSIREYEIVGKNYETLALTLYRSVGYLGKEDLVRRPGRPSGIK
LPTPDSQLLTEMTFEFALTSYSNDEDLSILAKEYLTPLVSYNKMPYNAMKLNDVDFFTPY
EYSLFEQESHLTLSTLKKAENEDRLVLRVFNTCKENQSLKLNIPLENTINLNEEHIAFDN
TILYNQVKSFLIKK

Enzyme Prediction     

No EC number prediction in MGYG000001635_00106.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	4	261	2.1e-76	0.9442379182156134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	0.0	1	853	2	875	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	7.51e-162	4	273	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.
COG0383	AMS1	1.57e-132	1	854	2	941	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10790	GH38N_AMII_1	3.63e-108	5	286	2	273	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.
cd10814	GH38N_AMII_SpGH38_like	9.99e-100	4	273	1	271	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQV04903.1	0.0	1	852	1	853
QQY28131.1	0.0	1	852	1	853
QPS13036.1	0.0	1	852	1	853
QMW73701.1	0.0	1	852	1	853
ALR90494.1	0.0	3	853	2	870

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	1.40e-100	3	816	7	854	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	1.60e-98	2	811	25	874	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	1.38e-96	3	816	7	854	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
5JM0_A	7.76e-15	5	646	304	890	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
6LZ1_A	5.32e-14	5	660	283	904	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	1.91e-297	2	811	4	821	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	1.99e-84	1	819	1	853	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	3.02e-16	5	354	252	595	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
Q9NTJ4	3.02e-16	5	349	253	591	Alpha-mannosidase 2C1 OS=Homo sapiens OX=9606 GN=MAN2C1 PE=1 SV=1
P21139	3.55e-15	5	354	252	595	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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001635_00106.