CAZyme Information: MGYG000002805_01151

Basic Information

• Species: CAG-488 sp900539465
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-488; CAG-488 sp900539465
• CAZyme ID: MGYG000002805_01151
• CAZy Family: GH38
• CAZyme Description: Mannosylglycerate hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
952		109259.95	5.1268

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002805	2212369	MAG	Peru	South America

• Gene Location: Start: 11636; End: 14494 Strand: +

Full Sequence      

MDKKDKQIQCHFISNTHWDREWRFSARRTQYMLGYMLDMLMDILEKYPEFRHFHLDSQTM
PVQDYLEVYPEKKELFKKYVSDGRIGIGPWFCLPDEFCVGGESLIRNLLLGHKIGKEMGG
ISKTGYSPFGWGQISQLPQIYAGFDIHFASFYRGVNEYNTPKSEFYWESPDGTRIYGSRL
GKRPRYNIWYVVQRPVYFNQSNENNRDMLWNDNNGAFKFIDSENGRLDYQYAHPFYEYHK
ENIKPRGEQAIKEQDNDWTTPHRFWSVGHDSSCPDAREVQMIKDLDEALPNAHVFHSTLK
EMEQGIIDDFDPSSPVIKGEMREPYTKGSVSAMMGWIISARTYIKQTNFDTERRLTNYAE
PMAVFASFCGAPYPQNFIDLSYNYLLQNHGHDSIGACGRDIVYEDVISRFRQSRELSVCV
FERAFMDVAGDIDLGSFDKNDAAIVIFNPAPTKRSEAVKISVELPAEWKADSFKIVDADG
NELKYQILATNMNNAQIIQNPNDVANVLHTQQYTIMLDVKDVPAMGYKTLKMQPLYHVRA
KNPVTMKKNAQTMENEYLRVTINANGTYDVLEKDTGKLFTSLGYFKDTGETGNPWEHIVP
ENDETFTTLNESAKITLLHEGELETSYKVVIDWALPEGRNMDEKTRSSHLKLFKIENIVT
LKKGSRYLEVETTVDNQSEDHYFQVAFPTNIKAEFVHAQGQFDVVKRPIKRPDYSLYDEI
PMTEHPMNSFVDISDGKQGVALLNTGLKAYEAADDECNTMYLSLLRSFPLRICVTSDMQD
YSGWDKGSQCIGKNTFRYAFMPHSGDWEEGKVWTESDNFNLTFSAAQLAPTDHGKNALEH
SFIELSDDTLSVSAVKRSEDGEGWIVRLFNPSDSAKTAKIRVNGGIAPIEKTQSPVERQL
TEFELPEYSGKKWSEAKLVSLEEKDVAPLTLDGDGFAEFEITGKKILTFKFM

Enzyme Prediction     

No EC number prediction in MGYG000002805_01151.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH38	10	304	5.9e-50	0.9144981412639405

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09819	PRK09819	8.76e-140	11	883	7	833	mannosylglycerate hydrolase.
COG0383	AMS1	5.22e-86	1	908	1	934	Alpha-mannosidase [Carbohydrate transport and metabolism].
cd10814	GH38N_AMII_SpGH38_like	6.84e-73	9	324	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.
cd10815	GH38N_AMII_EcMngB_like	3.21e-65	11	324	3	269	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	7.86e-44	11	177	3	169	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
AQQ70439.1	0.0	7	951	25	969
AQT69805.1	0.0	9	952	35	981
AFH48718.1	2.74e-220	2	891	3	893
AXA36681.1	1.13e-176	6	948	5	913
AIQ15502.1	6.57e-163	6	888	9	884

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KBP_A	5.86e-103	11	870	10	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]
3LVT_A	4.02e-99	11	870	10	849	TheCrystal Structure of a Protein in the Glycosyl Hydrolase Family 38 from Enterococcus faecalis to 2.55A [Enterococcus faecalis V583]
2WYH_A	1.57e-83	11	873	29	877	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P54746	3.77e-82	11	875	8	826	Mannosylglycerate hydrolase OS=Escherichia coli (strain K12) OX=83333 GN=mngB PE=1 SV=2
Q9KER1	5.09e-78	11	871	6	846	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	7.24e-17	5	877	252	1035	Alpha-mannosidase G OS=Dictyostelium discoideum OX=44689 GN=manG 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
1.000043	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002805_01151.