CAZyme Information: MGYG000001504_00772

Basic Information

• Species: Mt11 sp001282665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Tepidimicrobiaceae; Mt11; Mt11 sp001282665
• CAZyme ID: MGYG000001504_00772
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
884	MGYG000001504_13|CGC1	103216.25	4.9078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001504	3566389	Isolate	not provided	not provided

• Gene Location: Start: 303910; End: 306564 Strand: +

Full Sequence      

MKKLKIGIIPHTHWDREWYFTSSKSMIYSLHNFNEIIEHLEKDEEFKCFVLDGQTSIIED
YLMMNPHMENRVKKLVKDNRLITGPWYTQPDTLVVSGESLIRNLLYGTRKARELGRTMEV
GYLPDSFGMSEQMPQIYRGFGFKYATFRRGIADRLVKKGEFYWSSPNGDEVFVHNIYAYG
SIGYPPENPEEIKEFMLKTIDKLEDKYDTGLILLFNGEDQKPIRKNLPQIINTAREVLPD
IDFEIMSIEEGLIELEKSNMDFERYKGELTFGQYSRTHKSIFSTRADLKIMNNRMENYIQ
NIVEPILSIAYSLGFRYEDKVLEKIWKLMLDNSAHDSIGMCNSDATNRDVEHRFIEAKNL
STSLAELKLREISTKIPVKDNFQFQVYNLLPYARGKLLETQIFLPSKEVEIYDDEGNIYS
SEIIEIKDVTEDILKKSIREIGVDNDSSTNWHKEIKKIYDANILIDIKELPPMGYKTLYI
REKSNSRNLETKDIDYIENEYFTVSIDDNGIIDIFDKMKDRRYSDAIYFEDDGDEGDSYD
YSEPNDNIYLRDINVIDTKISSNSLKSIMHIKFEMPLPYNLKERSEGKISVDNIIEMDIS
LIKGSPNIEIDISILNRAIEHRLRLIVNTEIYAKSSYADEQFGTIKREVYLEEVEYWREQ
GWNEKPRTIEPMQSFAAIKDEDLAVQVITDSVREYQIIGENYNKIAMTILRSTPLLGKEE
LNDRPGRESGTKAPTPDAELMNKKIHARYFIRYYSKFNPYEFAKNAKEILTPIVSYQGSQ
FKNNTTYFVITNPKDKNLNPNYSLFELKGDAILSTVKKVEDKDDLIIRFFNPDRNYNKDA
EIVGTNAILYEARLDEKPISKLEENTIEIGTCEAKTIIYHRIVK

Enzyme Prediction     

No EC number prediction in MGYG000001504_00772.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	6	260	5.1e-68	0.9405204460966543

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	0.0	1	879	1	874	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	3.29e-124	5	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	1.82e-107	1	877	1	939	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10814	GH38N_AMII_SpGH38_like	3.36e-83	5	270	1	268	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	2.03e-65	5	286	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QAT60679.1	0.0	1	879	1	879
BBM35225.1	1.03e-271	2	867	7	871
ACZ10787.1	5.32e-267	2	869	3	879
ALA96367.1	8.90e-267	2	877	7	898
QUH29622.1	3.66e-264	5	870	6	880

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	1.43e-73	1	717	4	758	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	5.46e-71	1	881	23	922	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	3.59e-70	3	717	6	758	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
5JM0_A	3.74e-13	9	341	307	646	Structureof the S. cerevisiae alpha-mannosidase 1 [Saccharomyces cerevisiae S288C]
6LZ1_A	9.96e-12	3	401	280	684	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	2.81e-169	5	856	6	848	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	7.43e-70	8	869	7	883	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
Q54K67	1.63e-17	5	712	256	939	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG PE=1 SV=1
Q91W89	6.22e-17	6	398	252	637	Alpha-mannosidase 2C1 OS=Mus musculus OX=10090 GN=Man2c1 PE=1 SV=1
P21139	2.86e-15	11	341	257	583	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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001504_00772.